The hows and whys of aerobic H-2 metabolism

TY - JOUR

T1 - The hows and whys of aerobic H-2 metabolism

A1 - Parkin,Alison

A1 - Sargent,Frank

AU - Parkin,Alison

AU - Sargent,Frank

PY - 2012/4

Y1 - 2012/4

N2 - <p>The bacterial [NiFe]-hydrogenases have been classified as either 'standard' or 'O-2-tolerant' based on their ability to function in the presence of O-2. 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 O-2 attack. In light of recent structural data and mutagenic studies this article reviews the molecular mechanism of O-2-tolerance in [NiFe]-hydrogenases and discusses the biosynthesis of the unique Fe-S relay.</p>

AB - <p>The bacterial [NiFe]-hydrogenases have been classified as either 'standard' or 'O-2-tolerant' based on their ability to function in the presence of O-2. 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 O-2 attack. In light of recent structural data and mutagenic studies this article reviews the molecular mechanism of O-2-tolerance in [NiFe]-hydrogenases and discusses the biosynthesis of the unique Fe-S relay.</p>

U2 - 10.1016/j.cbpa.2012.01.012

DO - 10.1016/j.cbpa.2012.01.012

M1 - Scientific review

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

SN - 1367-5931

IS - 1-2

VL - 16

SP - 26

EP - 34

ER -