Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Link
http://www.nature.com/articles/ncomms16115.pdf
Reference39 articles.
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2. Cornish, A. J., Gartner, K., Yang, H., Peters, J. W. & Hegg, E. L. Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum. J. Biol. Chem. 286, 38341–38347 (2011).
3. Morra, S. et al. Site saturation mutagenesis demonstrates a central role for cysteine 298 as proton donor to the catalytic site in CaHydA [FeFe]-hydrogenase. PLoS ONE 7, e48400 (2012).
4. Berggren, G. et al. Biomimetic assembly and activation of [FeFe]-hydrogenases. Nature 499, 66–69 (2013).
5. Silakov, A., Wenk, B., Reijerse, E. & Lubitz, W. (14)N HYSCORE investigation of the H-cluster of [FeFe] hydrogenase: evidence for a nitrogen in the dithiol bridge. Phys. Chem. Chem. Phys. 11, 6592–6599 (2009).
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