TY - JOUR
T1 - The hows and whys of aerobic H2 metabolism
AU - Parkin, Alison
AU - Sargent, Frank
N1 - Copyright © 2012 Elsevier Ltd. All rights reserved.
PY - 2012/4
Y1 - 2012/4
N2 - The bacterial [NiFe]-hydrogenases have been classified as either 'standard' or 'O2-tolerant' based on their ability to function in the presence of O2. Typically, these enzymes contain four redox-active metal centers: a Ni-Fe-CO-2CN- active site and three electron-transferring Fe-S clusters. Recent research suggests that, rather than differences at the catalytic active site, it is a novel Fe-S cluster electron transfer (ET) relay that controls how [NiFe]-hydrogenases recover from O2 attack. In light of recent structural data and mutagenic studies this article reviews the molecular mechanism of O2-tolerance in [NiFe]-hydrogenases and discusses the biosynthesis of the unique Fe-S relay.
AB - The bacterial [NiFe]-hydrogenases have been classified as either 'standard' or 'O2-tolerant' based on their ability to function in the presence of O2. Typically, these enzymes contain four redox-active metal centers: a Ni-Fe-CO-2CN- active site and three electron-transferring Fe-S clusters. Recent research suggests that, rather than differences at the catalytic active site, it is a novel Fe-S cluster electron transfer (ET) relay that controls how [NiFe]-hydrogenases recover from O2 attack. In light of recent structural data and mutagenic studies this article reviews the molecular mechanism of O2-tolerance in [NiFe]-hydrogenases and discusses the biosynthesis of the unique Fe-S relay.
UR - http://www.scopus.com/inward/record.url?scp=84859638884&partnerID=8YFLogxK
U2 - 10.1016/j.cbpa.2012.01.012
DO - 10.1016/j.cbpa.2012.01.012
M3 - Article
C2 - 22366384
VL - 16
SP - 26
EP - 34
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
IS - 1-2
ER -