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Spectroscopic insight into the mechanism of nickel‐substituted rubredoxin, a bioinspired hydrogenase mimic
Author(s) -
Stevenson Michael James,
Slater Jeffrey Worthington,
Marguet Sean Conrad,
Shafaat Hannah S
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.764.3
Subject(s) - hydrogenase , rubredoxin , catalysis , nickel , chemistry , combinatorial chemistry , hydride , cysteine , enzyme , hydrogen , crystallography , biochemistry , organic chemistry
Nickel‐substituted rubredoxin (NiRd) has been shown to serve as a functional mimic of nickel‐containing hydrogenases, able to produce hydrogen gas with high catalytic rates. In the native enzyme, the nickel center is coordinated by four cysteine thiolates. A similar environment is seen in NiRd, which represents the first functional model to reproduce this coordination motif. This 52‐residue protein is stable under a wide range of conditions, making it well‐suited for catalytic hydrogen production or in future fuel cells. Although much is known about the structure and function of native rubredoxin and its variants, the catalytic mechanism for hydrogen generation remains unknown. It has been postulated that NiRd may follow a similar mechanism to the well‐studied [NiFe] hydrogenase, with a terminal, rather than a bridging, hydride on the nickel(III) center. Using multiple spectroscopic methods, structures of key catalytic intermediates have been elucidated and compared to those reported for the native [NiFe] hydrogenase. This study of NiRd not only resolves the mechanistic details of an efficient, robust, bioinspired catalyst, but also provides insight into proposed intermediates of the [NiFe] hydrogenase. Support or Funding Information The Ohio State University, The Institute for Materials Research, The National Science Foundation