Generating single metalloprotein crystals in well-defined redox states: electrochemical control combined with infrared imaging of a NiFe hydrogenase crystal†
P. A.
Ash, 
a
H. A.
Reeve,
a
J. S.
Rowbotham,
a
R. M.
Evans,
a
F. A.
Armstrong
a
and
K. A.
Vincent
*a
a
H. A.
Reeve,
a
J. S.
Rowbotham,
a
R. M.
Evans,
a
F. A.
Armstrong
a
and
K. A.
Vincent
*a
Abstract
We describe an approach to generating and verifying well-defined redox states in metalloprotein single crystals by combining electrochemical control with synchrotron infrared microspectroscopic imaging. For NiFe hydrogenase 1 from Escherichia coli we demonstrate fully reversible and uniform electrochemical reduction from the oxidised inactive to the fully reduced state, and temporally resolve steps during this reduction.
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