Mendel's Garden #14

 

Mendel's Garden #14 has been posted on Epigenetic News.

Nobel Laureate: Walther Hermann Nernst

 

The Nobel Prize in Chemistry 1920.

"in recognition of his work in thermochemistry"

Walther Hermann Nernst won the Nobel Prize in 1920 for his work in understanding the energy of reactions. The main work is summarized in the presentation speech,

Before Nernst began his actual thermochemical work in 1906, the position was as follows. Through the law of the conservation of energy, the first fundamental law of the theory of heat, it was possible on the one hand to calculate the change in the evolution of heat with the temperature. This is due to the fact that this change is equal to the difference between the specific heats of the original and the newly-formed substances, that is to say, the amount of heat required to raise their temperature from 0° to 1° C. According to van't Hoff, one could on the other hand calculate the change in chemical equilibrium, and consequently the relationship with temperature, if one knew the point of equilibrium at one given temperature as well as the heat of reaction.

The big problem, however, that of calculating the chemical affinity or the chemical equilibrium from thermochemical data, was still unsolved.

With the aid of his co-workers Nernst was able through extremely valuable experimental research to obtain a most remarkable result concerning the change in specific heats at low temperatures.

That is to say, it was shown that at relatively low temperatures specific heats begin to drop rapidly, and if extreme experimental measures such as freezing with liquid hydrogen are used to achieve temperatures approaching absolute zero, i.e. in the region of -273° C, they fall almost to zero.

This means that at these low temperatures the difference between the specific heats of various substances comes even closer to zero, and thus that the heat of reaction for solid and liquid substances practically becomes independent of temperature at very low temperatures.

Today, Nernst is known for his other contributions to thermodynamics. In biochemistry he is responsible for the Nernst equation that relates standard reduction potentials and Gibbs free energy.

The Nernst Equation

 
In standard oxidation-reduction reactions you can usually tell whether a given compound will donate or receive electrons by looking at the standard reduction potential (ΔE°ʹ) [Oxidation-Reduction Reactions]. This is a big step toward understanding how electrons flow in biochemical reactions but we would like to know more about the energy of oxidation-reduction reactions since they are the fundamental energy-producing reactions in the cell.

The standard reduction potential for the transfer of electrons from one molecular species to another is related to the standard Gibbs free energy change (ΔG°ʹ) for the oxidation-reduction reaction by the equation

where n is the number of electrons transferred and ℱ (F) is Faraday’s constant (96.48 kJ V^-1 mol^-1). ΔE°ʹ is defined as the difference in volts between the standard reduction potential of the electron-acceptor system and that of the electron-donor system. The Δ (delta) symbol indicates a change or a difference between two values.

You may recall that electrons tend to flow from half-reactions with a more negative standard reduction potential to those with a more positive one. For example, in the pyruvate dehydrogenase reaction electrons flow from pyruvate (E°' = -0.48 V) to NAD⁺ (E°' = -0.32 V). We can calculate the change in standard reduction potentials; it's equal to +0.16 V [-0.32 - (-0.48) = +0.16].

Now we can calculate a standard Gibbs free energy change (ΔG°ʹ) for the electron transfer part of the pyruvate dehydrogenase reaction. Two electrons are transferred from pyruvate to NAD⁺ so the standard Gibbs free energy change is -31 kJ mol^-1 [-2(96.48)(0.16)]. This turns out to be a significant amount of energy that could be captured by the NADH molecule but you have to keep in mind that this is a standard Gibbs free energy change and conditions inside the cell are far from standard. The biggest difference is that standard Gibbs free energy changes are computed with equal concentrations of reactants and products at a concentration of 1M—about a thousand times higher than the concentrations inside the cell where, in addition, the concentrations of reactants and products are not equal.

Fortunately, we have a way of adjusting the values of the Gibbs free energy change and the change in the standard reduction potential to account for the actual concentrations inside the cell. The standard Gibbs free energy change is related to the equilibrium constant of a reaction K_eq by the equation

Just as the actual Gibbs free energy change for a reaction is related to the standard Gibbs free energy change by this equation, an observed difference in reduction potentials (ΔE) is related to the difference in the standard reduction potentials (ΔE°') by the Nernst equation.

By combining equations for ΔG°ʹ we get
For a reaction involving the oxidation and reduction of two molecules, A and B,
the Nernst equation is
where [A_ox] is the concentration of oxidized A inside the cell. The Nernst equation tells us the actual difference in reduction potential (ΔE) and not the artificial standard change in reduction potential (ΔE°ʹ).

At 298 K (25° C), this equation reduces to
where Q represents the ratio of the actual concentrations of reduced and oxidized species. To calculate the electromotive force of a reaction under nonstandard conditions, use the Nernst equation and substitute the actual concentrations of reactants and products. Keep in mind that a positive E value indicates that an oxidation-reduction reaction will have a negative value for the standard Gibbs free energy change.

The Nernst equation is very famous but it's actually not very useful. The problem is that many of the oxidation-reduction reactions take place within an enzyme complex such as the pyruvate dehydrogenase complex. The concentrations of the reactants and products are difficult to calculate under such conditions. That's why we usually use the standard reduction potentials instead of the actual reduction potentials, keeping in mind that these are only approximations of what goes on inside the cell.

Let's see what happens when we calculate the standard Gibbs free energy change for the reaction where NADH donates electrons to oxygen. Oxygen serves as an electron sink for getting rid of excess electrons [Oxidation-Reduction Reactions].

NAD⁺ is reduced to NADH in coupled reactions where electrons are transferred from a metabolite (e.g., pyruvate) to NAD⁺. The reduced form of the coenzyme (NADH) becomes a source of electrons in other oxidation-reduction reactions. The Gibbs free energy changes associated with the overall oxidation-reduction reaction under standard conditions can be calculated from the standard reduction potentials of the two half-reactions using the equations above.

As an example, let’s consider the reaction where NADH is oxidized and molecular oxygen is reduced. This represents the available free energy change during membrane-associated electron transport. This free energy is recovered in the form of ATP synthesis.

The two half-reactions from a table of standard reduction potentials are,

and
Since the NAD⁺ half-reaction has the more negative standard reduction potential, NADH is the electron donor and oxygen is the electron acceptor. The net reaction is
and the change in standard reduction potential is

Using the equations described above we get

What this tells us is that a great deal of energy can be released when electrons are passed from NADH to oxygen provided the conditions inside the cell resemble those for the standard reduction potentials (they do). The standard Gibbs free energy change for the formation of ATP from ADP + P_i is -32 kJ mol^-1 (the actual free-energy change is greater under the conditions of the living cell, it's about -45 kJ mol^-1). This strongly suggests that the energy released during the oxidation of NADH under cellular conditions is sufficient to drive the formation of several molecules of ATP. Actual measurements reveal that the oxidation of NADH can be connected to formation of 2.5 molecules of ATP giving us confidence that the theory behind oxidation-reduction reactions is sound.

[©Laurence A. Moran. Some of the text is from Principles of Biochemistry 4th ed. ©Pearson/Prentice Hall]

A Rational Canadian Speaks Out

 
Dan Gardner wrote a column in the Ottawa Citizen [Those fanatical atheists]. He makes so much sense I'm just going to quote several paragraphs and let everyone see what every rational person should be saying. This is the effect Richard Dawkins is having and I think it's about time.

Then there's the problem on the other side -- among the atheists such as Richard Dawkins who have been labelled "fanatics." Now, it is absolutely true that Dawkins' tone is often as charming as fingernails dragged slowly down a chalkboard. But just what is the core of Dawkins' radical message?

Well, it goes something like this: If you claim that something is true, I will examine the evidence which supports your claim; if you have no evidence, I will not accept that what you say is true and I will think you a foolish and gullible person for believing it so.

That's it. That's the whole, crazy, fanatical package.

When the Pope says that a few words and some hand-waving causes a cracker to transform into the flesh of a 2,000-year-old man, Dawkins and his fellow travellers say, well, prove it. It should be simple. Swab the Host and do a DNA analysis. If you don't, we will give your claim no more respect than we give to those who say they see the future in crystal balls or bend spoons with their minds or become werewolves at each full moon.

And for this, it is Dawkins, not the Pope, who is labelled the unreasonable fanatic on par with faith-saturated madmen who sacrifice children to an invisible spirit.

This is completely contrary to how we live the rest of our lives. We demand proof of even trivial claims ("John was the main creative force behind Sergeant Pepper") and we dismiss those who make such claims without proof. We are still more demanding when claims are made on matters that are at least temporarily important ("Saddam Hussein has weapons of mass destruction" being a notorious example).

So isn't it odd that when claims are made about matters as important as the nature of existence and our place in it we suddenly drop all expectation of proof and we respect those who make and believe claims without the slightest evidence? Why is it perfectly reasonable to roll my eyes when someone makes the bald assertion that Ringo was the greatest Beatle but it is "fundamentalist" and "fanatical" to say that, absent evidence, it is absurd to believe Muhammad was not lying or hallucinating when he claimed to have long chats with God?

[Hat Tip: PZ Myers]

Oxidation-Reduction Reactions

 
Biochemical reactions are just a complicated form of organic chemistry. Living organisms have evolved enzymes that make these reactions go faster but the underlying chemistry is unchanged.

Cells are constantly having to deal with the problem of shuffling electrons and channeling them to the right place. You might be familiar with the classic fuel metabolism example of glycolysis where the breakdown of glucose to CO₂ releases electrons. When a reaction results in the loss of electrons it's called an oxidation reaction. When electrons are gained it's a reduction reaction. Oxidations and reductions always go together since electrons are passed from one molecule to another.


Loss of Electrons is Oxidation (LEO)


Gain of Electrons is Reduction (GER)


LEO says GER


Oxidation Is Loss of electrons (OIL)


Reduction Is Gain of electrons (RIG)


OIL RIG

During glycolysis, the electrons that are released have to be deposited in some sort of electron sink and expelled as waste. If a cell couldn't get rid of its electrons it would build up a huge negative charge.

Oxygen is the electron sink in mammalian fuel metabolism. A molecule of oxygen takes up electrons and combines with protons to make water. The easiest way to see this is to draw the molecules as Lewis structures showing the valence electrons (Pushing Electrons).

There are sixteen electron on each side of this equation for the reduction of molecular oxygen. Remember, reduction is a gain of electrons. This is a half-reaction, there is no corresponding oxidation that provides the electrons so this isn't a valid oxidation-reduction reaction. It just shows the reduction part.

None of the reactions of glycolysis result in the direct reduction of molecular oxygen. In all cases, the release of electrons when glucose is broken down to CO₂ is coupled to temporary electron storage in various coenzymes. We have already encountered several of these electron storage molecules such as ubiquinone, FMN & FAD, and NADPH.

We discussed a simple electron transport chain where electrons were passed from pyruvate to NAD⁺ in the pyruvate dehydrogenase reaction. This is a classic oxidation-reduction reaction.

How do we know which direction electron are going to flow? For example, if ubiquinone is reduced to ubiquinol by acquiring two electrons then where do the electrons come from? Can NADH pass electrons to ubiquinone or does ubiquinol pass its two electrons to NAD⁺? And where does FAD⁺ fit? Can it receive electrons from NADH?

The answer is related to the reduction potential of the various electron carriers. In order to understand reduction potentials we need to learn a little inorganic chemistry.

The reduction potential of a reducing agent is a measure of its thermodynamic reactivity. Reduction potential can be measured in electrochemical cells. An example of a simple inorganic oxidation-reduction reaction is the transfer of a pair of electrons from a zinc atom (Zn) to a copper ion (Cu²⁺) as shown below. When a pair of electrons is removed from zinc it leaves a zinc ion that's deficient in two negative charges (Zn²⁺). These electrons can be taken up by a copper ion (Cu²⁺) resulting in a copper atom (Cu) with no charge.

This reaction can be carried out in two separate solutions that divide the overall reaction into two half-reactions. At the zinc electrode, two electrons are given up by each zinc atom that reacts (the reducing agent). The electrons flow through a wire to the copper electrode, where they reduce Cu2+ (the oxidizing agent) to metallic copper. A salt bridge, consisting of a tube with a porous partition filled with electrolyte, preserves electrical neutrality by providing an aqueous path for the flow of nonreactive counterions between the two solutions. The flow of ions and the flow of electons are separated in an electrochemical cell. Electron flow (i.e., electric energy) can be measured using a voltmeter.
The direction of the current through the circuit in the figure indicates that Zn is more easily oxidized than Cu (i.e., Zn is a stronger reducing agent than Cu). The reading on the voltmeter represents a potential difference—the difference between the reduction potential of the reaction on the left and that on the right. The measured potential difference is the electromotive force.

It is useful to have a reference standard for measurements of reduction potentials just as in measurements of Gibbs free energy changes. For reduction potentials, the reference is not simply a set of reaction conditions but a reference half-reaction to which all other half-reactions can be compared. The reference half-reaction is the reduction of H+ to hydrogen gas (H2). The reduction potential of this half-reaction under standard conditions (E̊) is arbitrarily set at 0.0 V. The standard reduction potential of any other half-reaction is measured with an oxidation-reduction coupled reaction in which the reference half-cell contains a solution of 1M H+ and 1 atm H2(gaseous), and the sample half-cell contains 1 M each of the oxidized and reduced species of the substance whose reduction potential is to be determined. Under standard conditions for biological measurements, the hydrogen ion concentration in the sample half-cell is (pH 7.0). The voltmeter across the oxidation-reduction couple measures the electromotive force, or the difference in the reduction potential, between the reference and sample half-reactions. Since the standard reduction potential of the reference half-reaction is 0.0 V, the measured potential is that of the sample half-reaction.
The table below gives the standard reduction potentials at pH 7.0 (E̊́) of some important biological half-reactions. Electrons flow spontaneously from the more readily oxidized substance (the one with the more negative reduction potential) to the more readily reduced substance (the one with the more positive reduction potential). Therefore, more negative potentials are assigned to reaction systems that have a greater tendency to donate electrons (i.e., systems that tend to oxidize most easily).

It's important to note the direction of all these reactions is written in the form of a reduction or gain of electrons. That's not important when it comes to determining the direction of electron flow. For example, note that the reduction of acetyl-CoA to pyruvate is at the top of the list (E̊́= -0.48 V). This is the reaction catalyzed by pyruvate dehydrogenase. Electrons released by the oxidation of pyruvate will flow to any half reaction that has a higher (less negative) standard reduction potential. In this case the electrons end up in NADH (E̊́ = -0.32 V).

The reduction of oxygen is way down at the bottom of the list. That's why it's an effective electron sink for gettng rid of electrons.

Now we'd like to know something about the thermodynamics of these electron transport reactions so we can find out how much energy is available to do useful work. This will lead us to the Nobel Laureate for April 25th.

[©Laurence A. Moran. Some of the text is from Principles of Biochemistry 4th ed. ©Pearson/Prentice Hall]

Pushing Electrons

 
Biochemistry, as the name implies, is concerned with the chemistry of life. The chemistry part is mostly organic chemistry and organic chemistry is mostly about pushing electrons.

Covalent bonds are formed when the nuclei of two atoms share a pair of electrons. The "bond" is actually a cloud of electrons orbiting the two nuclei. The atoms are held together because neither one is stable without the shared electrons. The reactions in organic chemistry and biochemistry can be thought of as simple rearrangements of electrons to form new covalent bonds and break apart old ones. In this sense it's all about pushing electrons from one location to another.

The best way to think about covalent bonds is to visualize the electrons in the other shell of atoms. Those are the ones that participated in bonding. The outer shell electrons are often referred to as the valence electrons. The first shell of electrons can only hold two electrons. Hydrogen atoms have a single electron so in order to form a stable compound they have to combine with something that supplies an electron that can be shared. The simplest of these compounds is a molecule of hydrogen (H₂).

When two atoms of hydrogen combine to form H₂ both atoms succeed in filling their outer shells with two electron by sharing electrons. The shared pair of electrons is the covalent bond. The type of structures shown in the equation are called Lewis Structures. The dots represent electrons in the outer shell of the atom.

The inner electron shell can only hold two electrons but all other shells can accommodate eight electrons. The atomic number of oxygen is 8, which means that it has two electrons in the inner shell and only six in the outer shell. It needs to combine with two other atoms in order to get enough electrons to fill the outer shell.
In this example, oxygen with six electrons in the valence shell is combining with two hydrogen atoms to form water (H₂O). By sharing electrons both the hydrogen atoms and the oxygen atom will complete their outer shells of electrons—hydrogen with two electrons and oxygen with eight.

Sometimes atoms can share more than a pair of electrons. For example, when two atoms of oxygen combine to form the oxygen molecule (O₂) there are four electrons shared between the two atoms. This results in a double bond between them.
Carbon has an atomic number of 6, which means that it has two electrons in the inner shell and only four electrons in the outer shell. Carbon can combine with four other atoms to fill up its outer shell with eight electrons. This ability to combine with several different atoms is one of the reasons why carbon is such a versatile atom. The structure of ethanol (CH₃CH₂OH, left) illustrates this versatility. Note that each atom has a complete outer shell of electrons and that each carbon atom is covalently bonded to four other atoms.

Biochemical reactions are a lot more complicated but once you understand the concept of electron pushing it becomes relatively easy to make sense of the reaction mechanisms seen in textbooks. The only additional information you need is the knowledge that some atoms can carry an extra electron and this makes them a negatively charged ion (e.g., — O^-). Some stable atoms are missing an electron in their outer shell so this makes them a positively charged ion (e.g., — N⁺).

In many cases a proton (H⁺) is released from a compound leaving its electron behind. This proton has to combine with an atom that already has a pair of electrons in its outer shell (e.g., a base B:). Here's an example of the reaction mechanism for aldolase, one of the enzymes in the gluconeogenesis/glycolysis pathway.
The outline of the enzyme is shown in blue. One of the key concepts in biochemistry is that enzymes speed up reactions, in part, by supplying and storing electrons. In this case an electron withdrawing group (X) pulls electrons from oxygen and this weakens the carbon-oxygen double bond (keto group). Carbon #2, in turn, pulls an electron from carbon #3 weakening the C3-C4 bond that will be broken. (Aldolase cleaves a six-carbon compound into two three-carbon compounds as shown here. It also preforms the reverse reaction where two three-carbon compounds are combined to form a six-carbon compound.)

A basic residue in the protein (B) removes a proton from the -OH (hydroxyl) group to form a B-H covalent bond. This leaves an additional electron on the oxygen and it combines with one left on C4 to from a double bond. The red arrows show the movement of electrons in these reaction mechanisms.

The key point here is that biochemical reactions are just like those of all chemical reactions. They involve the movement of electrons to break and form covalent bonds.

Canada's Secret Spy Coin

 
According to the US Defense Department, Canada is planting coins containing secret radio transmitters on US Defense contractors travelling in Canada ['Poppy quarter' behind spy coin alert]. The coins are the 2004 commemorative quarters issued to remember those who died in Canada's wars. The coins have a red poppy in the center [In Flanders Fields].

Here's what the Associated Press article says,

WASHINGTON - An odd-looking Canadian quarter with a bright red flower was the culprit behind a false espionage warning from the Defense Department about mysterious coins with radio frequency transmitters, The Associated Press has learned.
ADVERTISEMENT

The harmless "poppy quarter" was so unfamiliar to suspicious U.S. Army contractors traveling in Canada that they filed confidential espionage accounts about them. The worried contractors described the coins as "filled with something man-made that looked like nano-technology," according to once-classified U.S. government reports and e-mails obtained by the AP.

I can see why the contractors were confused. American coins and paper money are so boring they probably thought every country had boring money.

Actually it's all a ruse to direct the contractors' attention away from the real source of the radio transmitters. They're in Tim Hortons coffee.

[Hat Tip: Mustafa Mond, FCD]

Theme: The Three Domain Hypothesis

 
This is a series of postings that describe the Three Domain Hypothesis. The Three Domain Hypothesis is the idea that life is divided into three domains—bacteria, archaebacteria, and eukaryotes—and that the archaebacteria and eukaryotes share a common ancestor. An example of this tree of life is shown on the Dept. of Energy (USA) Joint Genome Initiative website [JGI Microbial Genomes] (left).

The hypothesis was promoted by Carl Woese in the 1980's but the pure form has now been abandoned and replaced with a “net of life” concept of early evolution as shown in the figure below. This figure is taken from Ford Doolittle's Scientific American article "Uprooting the Tree of Life" (February 2000). © Scientific American




The Three Domain Hypothesis (part 1) (Nov. 17, 2006 )

The Three Domain Hypothesis (part 2) (Nov. 22, 2006)

The Three Domain Hypothesis (part 3) (Nov. 26, 2006)

The Three Domain Hypothesis (part 4) (Nov. 29, 2006)

The Three Domain Hypothesis (part 5) (Dec. 8, 2006)

The Three Domain Hypothesis (part 6) Carl Woese (Dec. 31, 2006)

Now the IDiots Don't Get Evolution (Feb. 14, 2007)

The Web of Life (March 15, 2007)

Is "Prokaryote" a Useful Term? (October 4, 2007)

Celebrating the Three Domain Hypothesis (October 18, 2007)

The Tree of Life (May 22, 2008)

Sequence Alignment (June 22, 2008)

On the Origin of Eukaryotes (December 27, 2008)

The Tree of Life (July 29, 2009)

Perspectives on the Tree of Life: Ford Doolittle (July 30, 2009)

Perspectives on the Tree of Life: Day One (July 31, 2009)

Perspectives on the Tree of Life: Day Two (August 1, 2009)

Perspectrives of the Tree of Life: Day Three (August 7, 2009)

Monday's Molecule #25

 
Name this molecule. We need the exact name since it's pretty easy to guess one of the trivial names.

As usual, there's a connection between Monday's molecule and this Wednesday's Nobel Laureate(s). This one is dead easy—at least it will seem that way once you recognize the Nobel Prize winner(s). The reward (free lunch) goes to the person who correctly identifies both the molecule and the Nobel Laureate(s). (Previous free lunch winners are ineligible for one month from the time they first won. There is only one ineligible candidate for this Wednesday's reward.)

Comments will be blocked for 24 hours. Comments are now open.

Saving Bigfoot

 
Mike Lake is the Canadian member of parliament for Edmonton-Mill Woods-Beaumont. He belongs to the Conservative Party of Stephen Harper.

Lake is 38 years old and has a bachelor of commerce degree from the University of Alberta. In other words, he is a university graduate.

Lake calls for bigfoot to be protected under Canada's Species at Risk Act [Bigfoot risks extinction, says Canadian MP]. It appears that Mike Lake has been persuaded to make a fool of himself by bigfoot "researcher" Todd Standing. This should not be a surprise since all Conservative MP's have already demonstrated a certain amount of detachment from reality.

Canadians will get a kick out of another press release [Bigfoot May Gain Protection by Canadian Parliament] where Mike Lake MP is identified as a member of the Canadian Mounted Police.

[Hat Tip: fellow Canadian James Hrynyshyn]

Gene Genie #6

 
Read the sixth edition of Gene Genie at Scienceroll [Gene Genie: a Famous Blog Carnival’s Sixth Issue]. There's lots of good science but if that doesn't tempt you then go for the videos on Mendel and genetics.

My contributions are the articles on the genes for The Human Genes for the Pyruvate Dehydrogenase Complex and Noncoding DNA and Junk DNA.

What's Your Abel Number?

 
Pharmacologists at the recent Experimental Biology meeting in Washington were excited about their Abel numbers [Six degrees of pharmacology]. The Abel number represents the number of links to John J. Abel, the founder of modern pharmacology. In this case the links have to be through authors on a publication.

I wonder who we could choose for biochemistry?

They Put Nicotine in Tim Hortons Coffee

 
Friday's Urban Legend: FALSE

Have you received an email message like this one?

Are you a Non- Smoker or Against smoking all together ?

Do you ever wonder why you have to have your coffee every morning?

** TIM HORTON'S SHOCKER **

A man from Arkansas came up to Canada for a visit only to find himself in the hospital after a couple of days. Doctor's told him that he had suffered of cardiac arrest. He was allergic to Nicotine. The man did not understand why that would of happened as he does not smoke knowing full well he was allergic to Nicotine. He told the doctor that he had not done anything different while he was on vacation other than having Tim Horton's coffee. The man then went back to Tim Horton's and asked what was in their coffee. Tim Horton's refuses to divulge that information. After threatening legal action, Tim Horton's finally admitted.....

*** THERE IS NICOTINE IN TIM HORTON'S COFFEE ***

A girl I know was on the patch to quit smoking. After a couple of days she was having chest pains & was rushed to the hospital. The doctor told her that she was on a Nicotine overload. She swore up & down that she had not been smoking. SHE WAS HAVING HER COFFEE EVERY MORNING.

Now imagine a women who quits smoking because she finds out that she is pregnant, but still likes to have her Tim Horton's once in a while.

THIS IS NOT A JOKE, PLEASE PASS THIS ALONG.... YOU MIGHT SEE THIS ON THE NEWS SOON.

Another version has "them" putting MSG in the coffee instead of nicotine. That's the version that I received this week from well-meaning, but not very skeptical, friends.

As usual, snoopes.com is on the case [Nicotine Non-Fit]. There is no nicotine in Tim Hortons coffee and there's no MSG either.

I'm a "Modernist"

 

You scored as Modernist. Modernism represents the thought that science and reason are all we need to carry on. Religion is unnecessary and any sort of spirituality halts progress. You believe everything has a rational explanation. 50% of Americans share your world-view. Modernist 100% Materialist 88% Existentialist 81% Postmodernist 44% Romanticist 38% Idealist 31% Cultural Creative 25% Fundamentalist 0% What is Your World View? created with QuizFarm.com

[Hat Tip: Shalini]

USA Is Number 2 in Health Care

 
Scientific American, that paragon of science writing, has an article on health care. It reports the results of a study done by a bunch of Canadians. They compare the health care systems in the USA and Canada and discover that We're Number Two: Canada Has as Good or Better Health Care than the U.S..

According to Woolhandler, by looking at already ill patients, the researchers eliminated any Canadian lifestyle advantage and just examined the degree to which the two systems affected patient deaths. (Mortality was the one kind of data they could extract from a disparate pool of 38 papers examining everything from kidney failure to rheumatoid arthritis.)

Overall, the results favored Canadians, who were 5 percent less likely than Americans to die in the course of treatment. Some disorders, such as kidney failure, favored Canadians more strongly than Americans, whereas others, such as hip fracture, had slightly better outcomes in the U.S. than in Canada. Of the 38 studies the authors surveyed, which were winnowed down from a pool of thousands, 14 favored Canada, five the U.S., and 19 yielded mixed results.

These studies are never conclusive. There will always be people who quibble about this or that and just as you might expect there is the obligatory complaint about wait times in Canada.

The point isn't so much whether Canada is better—although it is—the point is that Americans have just got to stop pretending that they have the best health care system in the world. At the very least it's time to admit that it's "one of the best." One thing is very clear, the American system may not be the best in the world but it's sure the most expensive.

The study's authors highlight the fact that per capita spending on health care is 89 percent higher in the U.S. than in Canada. "One thing that people generally know is that the administration costs are much higher in the U.S.," Groome notes. Indeed, one study by Woolhandler published in The New England Journal of Medicine in 2003 found that 31 percent of spending on health care in the U.S. went to administrative costs, whereas Canada spent only 17 percent on the same functions.

I suspect there are many European countries with health care systems that are just as good as the one in America. I suspect that Japan, New Zealand, and Australia have good health care as well. I've never seen any data that shows that the quality of health care in America is better than everywhere else in the world. It seems to be one of those myths of American superiority that has no basis in fact. The myth prevents Americans from joining the rest of the civilized world and adopting socialized medicine.