TY - JOUR
T1 - Crystal Structure of the [FeFe]-Hydrogenase Maturase HydE Bound to Complex-B
AU - Rohac, Roman
AU - Martin, Lydie
AU - Liu, Liang
AU - Basu, Debashis
AU - Tao, Lizhi
AU - Britt, R. David
AU - Rauchfuss, Thomas B.
AU - Nicolet, Yvain
N1 - Funding Information:
R.R. and Y.N. thank the ESRF staff for their constant support during remote data collection despite the COVID-19 pandemic. R.R. and Y.N. also thank Pierre Legrand from SOLEIL for his help with data collection. This work was supported by the French National Research Agency in the framework of the Investissements d’Avenir program (ANR-15-IDEX-02) through the funding of the “Origin of Life” project of the Université Grenoble Alpes. This work used the platforms of the Grenoble Instruct-ERIC center (ISBG; UMS 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), which is supported by FRISBI (ANR-10-INBS-05-02) and GRAL and financed within the Université Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). This work was also supported by the National Institutes of Health Grant 1R35GM126961-01 to R.D.B and Grant GM61153 to T.B.R.
Publisher Copyright:
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PY - 2021/6/9
Y1 - 2021/6/9
N2 - [FeFe]-hydrogenases use a unique organometallic complex, termed the H cluster, to reversibly convert H2 into protons and low-potential electrons. It can be best described as a [Fe4S4] cluster coupled to a unique [2Fe]H center where the reaction actually takes place. The latter corresponds to two iron atoms, each of which is bound by one CN- ligand and one CO ligand. The two iron atoms are connected by a unique azadithiolate molecule (-S-CH2-NH-CH2-S-) and an additional bridging CO. This [2Fe]H center is built stepwise thanks to the well-orchestrated action of maturating enzymes that belong to the Hyd machinery. Among them, HydG converts l-tyrosine into CO and CN- to produce a unique l-cysteine-Fe(CO)2CN species termed complex-B. Very recently, HydE was shown to perform radical-based chemistry using synthetic complex-B as a substrate. Here we report the high-resolution crystal structure that establishes the identity of the complex-B-bound HydE. By triggering the reaction prior to crystallization, we trapped a new five-coordinate Fe species, supporting the proposal that HydE performs complex modifications of complex-B to produce a monomeric "SFe(CO)2CN"precursor to the [2Fe]H center. Substrate access, product release, and intermediate transfer are also discussed.
AB - [FeFe]-hydrogenases use a unique organometallic complex, termed the H cluster, to reversibly convert H2 into protons and low-potential electrons. It can be best described as a [Fe4S4] cluster coupled to a unique [2Fe]H center where the reaction actually takes place. The latter corresponds to two iron atoms, each of which is bound by one CN- ligand and one CO ligand. The two iron atoms are connected by a unique azadithiolate molecule (-S-CH2-NH-CH2-S-) and an additional bridging CO. This [2Fe]H center is built stepwise thanks to the well-orchestrated action of maturating enzymes that belong to the Hyd machinery. Among them, HydG converts l-tyrosine into CO and CN- to produce a unique l-cysteine-Fe(CO)2CN species termed complex-B. Very recently, HydE was shown to perform radical-based chemistry using synthetic complex-B as a substrate. Here we report the high-resolution crystal structure that establishes the identity of the complex-B-bound HydE. By triggering the reaction prior to crystallization, we trapped a new five-coordinate Fe species, supporting the proposal that HydE performs complex modifications of complex-B to produce a monomeric "SFe(CO)2CN"precursor to the [2Fe]H center. Substrate access, product release, and intermediate transfer are also discussed.
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U2 - 10.1021/jacs.1c03367
DO - 10.1021/jacs.1c03367
M3 - Article
C2 - 34048236
AN - SCOPUS:85108021072
VL - 143
SP - 8499
EP - 8508
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 22
ER -