TY - JOUR
T1 - How the oxygen tolerance of a [NiFe]-hydrogenase depends on quaternary structure
AU - Wulff, Philip
AU - Thomas, Claudia
AU - Sargent, Frank
AU - Armstrong, Fraser A.
N1 - Research was supported by the Biological and Biotechnological Sciences Research Council (Grants BB/H003878-1 and BB/I022309-1 to FAA and BB/H001190/1 and BB/I02008X/1 to FS) and St John’s College, Oxford through award of a Graduate Scholarship to PW. F.A.A. is a Royal Society-Wolfson Research Merit Award holder. We thank Christopher Day for collaboration with mass spectrometry experiments.
PY - 2016/3
Y1 - 2016/3
N2 - ‘Oxygen-tolerant’ [NiFe]-hydrogenases can catalyze H2 oxidation under aerobic conditions, avoiding oxygenation and destruction of the active site. In one mechanism accounting for this special property, membrane-bound [NiFe]-hydrogenases accommodate a pool of electrons that allows an O2 molecule attacking the active site to be converted rapidly to harmless water. An important advantage may stem from having a dimeric or higher-order quaternary structure in which the electron-transfer relay chain of one partner is electronically coupled to that in the other. Hydrogenase-1 from E. coli has a dimeric structure in which the distal [4Fe-4S] clusters in each monomer are located approximately 12 Å apart, a distance conducive to fast electron tunneling. Such an arrangement can ensure that electrons from H2 oxidation released at the active site of one partner are immediately transferred to its counterpart when an O2 molecule attacks. This paper addresses the role of long-range, inter-domain electron transfer in the mechanism of O2-tolerance by comparing the properties of monomeric and dimeric forms of Hydrogenase-1. The results reveal a further interesting advantage that quaternary structure affords to proteins.
AB - ‘Oxygen-tolerant’ [NiFe]-hydrogenases can catalyze H2 oxidation under aerobic conditions, avoiding oxygenation and destruction of the active site. In one mechanism accounting for this special property, membrane-bound [NiFe]-hydrogenases accommodate a pool of electrons that allows an O2 molecule attacking the active site to be converted rapidly to harmless water. An important advantage may stem from having a dimeric or higher-order quaternary structure in which the electron-transfer relay chain of one partner is electronically coupled to that in the other. Hydrogenase-1 from E. coli has a dimeric structure in which the distal [4Fe-4S] clusters in each monomer are located approximately 12 Å apart, a distance conducive to fast electron tunneling. Such an arrangement can ensure that electrons from H2 oxidation released at the active site of one partner are immediately transferred to its counterpart when an O2 molecule attacks. This paper addresses the role of long-range, inter-domain electron transfer in the mechanism of O2-tolerance by comparing the properties of monomeric and dimeric forms of Hydrogenase-1. The results reveal a further interesting advantage that quaternary structure affords to proteins.
KW - Electron transfer
KW - Hydrogen
KW - Hydrogenase
KW - Iron-sulfur clusters
KW - Quaternary structure
UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-84959488381&origin=resultslist&sort=plf-f&src=s&st1=How+the+oxygen+tolerance+of+a+[NiFe]-hydrogenase+depends+on+quaternary+structure&st2=&sid=DF72D9749B30C31AEF0AC5C6479F5E6F.wsnAw8kcdt7IPYLO0V48gA%3a660&sot=b&sdt=b&sl=95&s=TITLE-ABS-KEY%28How+the+oxygen+tolerance+of+a+[NiFe]-hydrogenase+depends+on+quaternary+structure%29&relpos=0&citeCnt=1&searchTerm=
U2 - 10.1007/s00775-015-1327-6
DO - 10.1007/s00775-015-1327-6
M3 - Article
C2 - 26861789
SN - 0949-8257
VL - 21
SP - 121
EP - 134
JO - JBIC Journal of Biological Inorganic Chemistry
JF - JBIC Journal of Biological Inorganic Chemistry
IS - 1
ER -