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• W2070737324 endingPage "15594" @default.
• W2070737324 startingPage "15581" @default.
• W2070737324 abstract "The unusual [4Fe–3S] cluster proximal to the active site plays a crucial role in allowing a class of [NiFe]-hydrogenases to function in the presence of O2 through its unique ability to undergo two rapid, consecutive one-electron transfers. This property helps to neutralize reactive oxygen species. Mechanistic details and the role of the medial and distal clusters remain unresolved. To probe the Fe–S relay, continuous wave and pulse electron paramagnetic resonance (EPR) studies were conducted on the O2-tolerant hydrogenase from Escherichia coli (Hyd-1) and three variants with point mutations at the proximal and/or medial clusters. Reduction potentials of the proximal ([4Fe–3S]5+/4+/3+) and medial ([3Fe–4S]+/0) clusters were determined by potentiometry. The medial [3Fe–4S]+/0 reduction potential is exceptionally high, implicating a mechanistic role in O2-tolerance. Numerous experiments establish that the distal cluster has a ground state S > 1/2 in all three variants and indicate that this is also the case for native Hyd-1. Concurrent with the Hyd-1 crystal structure, EPR data for the ‘superoxidized’ P242C variant, in which the medial cluster is ‘magnetically silenced’, reveal two conformations of the proximal [4Fe–3S]5+ cluster, and X-band HYSCORE spectroscopy shows two 14N hyperfine couplings attributed to one conformer. The largest, A(14N) = [11.5,11.5,16.0] ± 1.5 MHz, characterizes the unusual bond between one Fe (Fe4) and the backbone amide-N of cysteine-20. The second, A(14N) = [2.8,4.6,3.5] ± 0.3 MHz, is assigned to NC19. The 14N hyperfine couplings are conclusive evidence that Fe4 is a valence-localized Fe3+ in the superoxidized state, whose formation permits an additional electron to be transferred rapidly back to the active site during O2 attack." @default.
• W2070737324 created "2016-06-24" @default.
• W2070737324 creator A5013871801 @default.
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• W2070737324 creator A5085638660 @default.
• W2070737324 date "2012-09-04" @default.
• W2070737324 modified "2023-10-06" @default.
• W2070737324 title "EPR Spectroscopic Studies of the Fe–S Clusters in the O₂-Tolerant [NiFe]-Hydrogenase Hyd-1 from Escherichia coli and Characterization of the Unique [4Fe–3S] Cluster by HYSCORE" @default.
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• W2070737324 doi "https://doi.org/10.1021/ja307117y" @default.
• W2070737324 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22900997" @default.
• W2070737324 hasPublicationYear "2012" @default.
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