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Feedback 2010
Scientific blunder in DeWitt interview?
Potassium ion channel, hydrated ionic radii
Published: 21 August 2010 (GMT+10)
Fig. 2 from Nobel Prize press release, ref. 2. The KcsA K+ channel. Fully or partially
hydrated potassium ions (blue) are seen just below and above the selectivity filter.
In the selectivity filter, potassium ions are coordinated by oxygen atoms (black)
in the protein backbone. The channel is closed by a gate in the lower part(arrows).
The gate can be opened by sensor domains (not shown) that pull the gate open.
This week’s main feedback comes from one of our most persistent critics, Richard
M. from the USA, who has a doctorate in biology. He thinks that an error in ionic
chemistry was made in our interview with
neurologist Dr David DeWitt. The interviewer,
Ph.D. chemist Dr Jonathan Sarfati
shows the truth of the matter.
This interaction illustrates an important point: critics of biblical creation can
sometimes present a critique that seems impressive with its scientific-sounding
detail. However, even when you think this is clear-cut case for which there is no
possible answer, it is essential to hear the other side. As the Bible says in Proverbs 18:17, The one who states his case first seems
right, until the other comes and examines him. That is, a good rule of thumb is:
the biblioskeptic is always wrong.
We also publish a short positive feedback below from a university biology student, Nicholas P, USA, thanking this site for providing good answers to the evolutionary propaganda in his courses.
Just a quick observation on one of Dr. DeWitt’s points. He holds up the selectivity
of one of the several potassium ion channels (he doesn’t say which of the
many) as an example of the inadequacy of natural selection, citing an ionic selectivity
for a large ion (K+) versus that of a smaller ion (NA+),
a situation that he obviously considers anomalous. He has gotten the story backwards
– what matters in aqueous solution is the hydrated radius of the ion, not
the atomic radius. The hydrated radius for K+ is 0.53 nm, while that
for NA+ is 0.79 nm. So sodium is actually the larger ion functionally,
as has been known for years, and the channel selectivity mirrors this fact. There
is a very large literature on this subject, and it is an example of a situation
where the basics of the chemistry and physics provide a completely adequate explanation
for a phenomenon. If one is going to try to advance an argument on the basis of
“gee whiz” assertions, one should be sure of the facts. Flimsy arguments
weaken a case when the audience is aware of their flaws.
CMI’s Dr Jonathan Sarfati
writes:
Dear Dr M.,
You are certainly right that the trend in hydrated ion size is often the reverse
of the plain ion size: the smaller ion has a stronger electric field (from Coulomb’s
inverse square law), so it attracts a bigger hydration shell. This means it has
a lower mobility in water (see for example
this page), i.e. in ordinary aqueous chemistry.
But when it comes to ion channels, the hydration shell is removed, so the
ordinary ionic radius is what’s important, and the sodium ion really
is smaller. One paper from Nature stated (emphasis added):
Ion transport proteins must remove an ion’s hydration shell to coordinate
the ion selectively on the basis of its size and charge. To discover how the K+
channel solves this fundamental aspect of ion conduction, we solved the structure
of the KcsA K+ channel in complex with a monoclonal Fab antibody
fragment at 2.0 Å resolution. Here we show how the K+ channel
displaces water molecules around an ion at its extracellular entryway,
and how it holds a K+ ion in a square antiprism of water molecules
in a cavity near its intracellular entryway. Carbonyl oxygen atoms within the selectivity
filter form a very similar square antiprism around each K+ binding
site, as if to mimic the waters of hydration. The selectivity filter changes
its ion coordination structure in low K+ solutions. This structural
change is crucial to the operation of the selectivity filter in the cellular context,
where the K+ ion concentration near the selectivity filter varies
in response to channel gating.1
Indeed, ion channels were such an important discovery that two pioneers were awarded
the
Nobel Prize for Chemistry in 2003: Peter Agre and Roderick MacKinnon (one
of the authors of Ref. 1). The ‘Advanced Information’ press release stated (emphasis added):
Dr DeWitt was correct to state that the sodium ion is smaller in the relevant
conditions of ion transport across membranes.
The breakthrough came in 1998, when Roderick MacKinnon succeeded in determining
the first high-resolution structure of an ion channel, the KcsA K+
channel from Streptomyces lividans, (Doyle et al., 1998). The design of
the selectivity filter was seen to be perfectly adapted to the job of desolvating
potassium ions while keeping smaller sodium ions out, Fig.
2, thus explaining the high K+ selectivity and the high transport
rate. At higher resolution, hydrated potassium ions could even be seen in “hold
position” on both sides of the selectivity filter (Zhou et al., 2001b),
and it became clear that the selectivity filter is composed of a succession of K+
binding sites that each almost exactly mimics the hydration shell normally present
around a potassium ion.2
Thus Dr DeWitt was correct to state that the sodium ion is smaller in the
relevant conditions of ion transport across membranes.
Regards
(Dr) Jonathan Sarfati
Feedback on this article
Dr M. responded:
Thanks, Dr. Sarfati, for keeping both of us honest. But my gut feeling is that Dr. DeWitt was not thinking along the lines of your answer when he listed the phenomenon as an evidence of design. As you so rightly pointed out, the selectivity has its basis firmly within the confines of “naturalistic” science (as you would term it). I can’t see how it is an evidence of special design — it is no more miraculous than the H-O-H bond angle in water (which has also been touted as an evidence of special design).
Dr S. replies:
Thanks Dr M. I don’t know what lines Dr DeWitt was thinking on either. All we can go by is what he said, and as shown, it was accurate.
I think my computer works by naturalistic lines too, and its workings are totally explained by the properties of doped semiconductors etc. But it doesn’t follow that its hardware and software originated naturalistically.
Update: this year, new research on this channel shows that it has exquisite machinery, including a latch that rotates like an iris, as well as pulleys and switches.3
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To the Creation Ministries Team:
I can’t thank you enough for the work you are doing to expose the truth in science. I have battled with the evolution vs. creation controversy for months in my university biology classes. As a student, I felt intimidated by the evolutionists and what they presented as ‘evidence’ for evolution. After feeling particularly discouraged one day, I came across your site. The materials and information you provided through your site encouraged and strengthened my heart. I hope one day others like myself will be encouraged the same way I was when I came across your ministry. It is truly a blessing to have real scientists defend the Word of God with real science.
Once again thank you.
—Nicholas P., USA
Related articles
References and notes
- Zhou, Y., João H. Morais-Cabral, J.H., Kaufman, A.,
and MacKinnon, R.,
Chemistry of ion coordination and hydration revealed by a K+ channel
Fab complex at 2.0 Å resolution, Nature 414:43–48, 1 November 2001 | doi:10.1038/35102009. Return to text.
- Nobel Prize for Chemistry, 2003, ‘Advanced Information’ press release. Return to text.
- Clark, O.B. et al., Domain Reorientation and Rotation of an Intracellular Assembly Regulate Conduction in Kir Potassium Channels, Cell 141(6):1018–1029, 3 June 2010. See also Sherwin, F., Cells: Sophisticated and God-Designed, Acts & Facts 39(8):17, 2010. Return to text.
| Anthony P said “Thanks for your … website, it’s really easy to navigate and it is a massive bonus to be able to read back-issues of your magazines … without your ministry I probably wouldn’t be a Christian today. Thank you so much and keep up the good work.” So help us do just that!  | | |
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