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June 2010 | Vol. 2 | No. 6

Issue
Cover > Investigative
Eye > Research into a 'breakwater' that helps electron
transfer published in PNAS

Research into a 'breakwater' that helps electron transfer
published in PNAS

An interdisciplinary team of researchers
at the University of Calgary has found that amino acid
residues form a type of barrier to help in the process of
electron transfer between proteins.

Electron transfer between proteins is the cornerstone of
biological energy transfer. Every life-form uses this process
to convert food or sunlight into chemical energy.

The U of C researchers found that the electron travels over
a bridge made of a water molecule, while residues on one of
the proteins form a sort of 'molecular breakwater' to keep
other water molecules away while the electron travels across
the bridge.

"You don't want too many (water molecules around the
bridge) because it gets too crowded and they're all bumping
into each other and you can't get one to fit at just the right
position and the right angle (for the bridge) for any length
of time," says PhD student Nathan Babcock. "It's like being on
a crowded subway where you can’t get comfortable."

In artificial mutations with a faulty breakwater, the water
bridge is disrupted and the rate of electron transfer is
markedly reduced, he says.

Babcock and Aurelien de la Lande, now at the CNRS in
France, Jan Rezac, now at the Czech Academy of Science, Barry
Sanders, iCORE Chair of Quantum Information Science at U of C
and Dennis Salahub, Director of the Institute for
Biocomplexity and Informatics and Professor in the Department
of Chemistry at U of C co-authored a paper, Surface
residues dynamically organize water bridges to enhance
electron transfer between proteins that has been published
in the prestigious journal, Proceedings of the National
Academy of Science (PNAS).

"This raises the bar for biomolecular modeling", says
Salahub. "At a fundamental level, it is by far the most
detailed insight that has been obtained for the dynamic role
of water in this kind of electron transfer, or for that matter
any biochemical reaction."

Using the CHARMM molecular simulation computer program, the
research team examined a 40 nanosecond period of electronic
coupling of the proteins methylamine dehydrogenase and
amicyanin from the bacterium Paracoccus denitrificans.

"This is fundamental research but you can imagine how
studies like this can be applied to various genetically
modified organisms, and if you can gain control over some, you
can use it to either speed up or slow down a particular
reaction," says Salahub.

He says the work was made possible with the collaboration
of two of the U of C's interdisciplinary research institutes;
the Institute for Biocomplexity and Informatics (IBI) and the
Institute for Quantum Information Science (IQIS).

Babcock, whose background is in quantum information theory,
was pleased to do research at the union of these two
disciplines. "When you think of quantum mechanics, usually
you’re thinking solid state semi conductors, atoms trapped
with lasers, etc. It's usually cold laboratory stuff, not warm
globby biological stuff," says the PhD student.

"I think the union of biology and quantum mechanics is
very, very exciting."

Investigative eye

Research
into a 'breakwater' that helps electron transfer published
in PNAS

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