Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy

• Published in: Nature communications Vol. 6; no. 1; p. 7890
• Main Authors: Ogata, Hideaki, Krämer, Tobias, Wang, Hongxin, Schilter, David, Pelmenschikov, Vladimir, van Gastel, Maurice, Neese, Frank, Rauchfuss, Thomas B., Gee, Leland B., Scott, Aubrey D., Yoda, Yoshitaka, Tanaka, Yoshihito, Lubitz, Wolfgang, Cramer, Stephen P.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 10.08.2015; Nature Publishing Group
• Subjects: 119/118; 639/638/11; 639/638/45/535; 639/638/45/56; 639/638/92/607; Desulfovibrio vulgaris - enzymology; Electrons; Enzymes; Fourier transforms; Humanities and Social Sciences; Hydrogenase - chemistry; INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Magnetic Resonance Spectroscopy; multidisciplinary; Science; Science (multidisciplinary); California; United States > US; Illinois; Japan; Germany

The metabolism of many anaerobes relies on [NiFe]-hydrogenases, whose characterization when bound to substrates has proven non-trivial. Presented here is direct evidence for a hydride bridge in the active site of the 57 Fe-labelled fully reduced Ni-R form of Desulfovibrio vulgaris Miyazaki F [NiFe]-...