Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: insights into the puzzling difference between unready and ready oxidized inactive states

Sophie E Lamle; Simon P J Albracht; Fraser A Armstrong

doi:10.1021/ja047939v

Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: insights into the puzzling difference between unready and ready oxidized inactive states

J Am Chem Soc. 2004 Nov 17;126(45):14899-909. doi: 10.1021/ja047939v.

Authors

Sophie E Lamle¹, Simon P J Albracht, Fraser A Armstrong

Affiliation

¹ Department of Chemistry, Inorganic Chemistry Laboratory, Oxford University, South Parks Road, Oxford, OX1 3QR, England.

PMID: 15535717
DOI: 10.1021/ja047939v

Abstract

Dynamic electrochemical studies, incorporating catalytic voltammetry and detailed potential-step manipulations, provide compelling evidence that the oxidized inactive state of [NiFe]-hydrogenases termed Unready (or Ni-A) contains a product of partial reduction of O(2) that is trapped in the active site.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Aerobiosis
Bacterial Proteins / chemistry
Bacterial Proteins / metabolism
Chromatiaceae / enzymology*
Electrochemistry
Enzyme Activation
Hydrogenase / chemistry*
Hydrogenase / metabolism*
Oxidation-Reduction
Oxygen / chemistry*
Oxygen / metabolism*
Oxygen / pharmacology

Substances

Bacterial Proteins
nickel-iron hydrogenase
Hydrogenase
Oxygen