Unknown

Dataset Information

0

Synthetic Active Site Model of the [NiFeSe] Hydrogenase.


ABSTRACT: A dinuclear synthetic model of the [NiFeSe] hydrogenase active site and a structural, spectroscopic and electrochemical analysis of this complex is reported. [NiFe('S2Se2')(CO)3] (H2'S2Se2' = 1,2-bis(2-thiabutyl-3,3-dimethyl-4-selenol)benzene) has been synthesized by reacting the nickel selenolate complex [Ni('S2Se2')] with [Fe(CO)3bda] (bda = benzylideneacetone). X-ray crystal structure analysis confirms that [NiFe('S2Se2')(CO)3] mimics the key structural features of the enzyme active site, including a doubly bridged heterobimetallic nickel and iron center with a selenolate terminally coordinated to the nickel center. Comparison of [NiFe('S2Se2')(CO)3] with the previously reported thiolate analogue [NiFe('S4')(CO)3] (H2'S4' = H2xbsms = 1,2-bis(4-mercapto-3,3-dimethyl-2-thiabutyl)benzene) showed that the selenolate groups in [NiFe('S2Se2')(CO)3] give lower carbonyl stretching frequencies in the IR spectrum. Electrochemical studies of [NiFe('S2Se2')(CO)3] and [NiFe('S4')(CO)3] demonstrated that both complexes do not operate as homogenous H2 evolution catalysts, but are precursors to a solid deposit on an electrode surface for H2 evolution catalysis in organic and aqueous solution.

SUBMITTER: Wombwell C 

PROVIDER: S-EPMC4510704 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Synthetic Active Site Model of the [NiFeSe] Hydrogenase.

Wombwell Claire C   Reisner Erwin E  

Chemistry (Weinheim an der Bergstrasse, Germany) 20150402 22


A dinuclear synthetic model of the [NiFeSe] hydrogenase active site and a structural, spectroscopic and electrochemical analysis of this complex is reported. [NiFe('S2Se2')(CO)3] (H2'S2Se2' = 1,2-bis(2-thiabutyl-3,3-dimethyl-4-selenol)benzene) has been synthesized by reacting the nickel selenolate complex [Ni('S2Se2')] with [Fe(CO)3bda] (bda = benzylideneacetone). X-ray crystal structure analysis confirms that [NiFe('S2Se2')(CO)3] mimics the key structural features of the enzyme active site, inc  ...[more]

Similar Datasets

| S-EPMC6354737 | biostudies-literature
| S-EPMC6095454 | biostudies-literature
| S-EPMC5555595 | biostudies-literature
| S-EPMC3340144 | biostudies-literature
| S-EPMC1557583 | biostudies-literature
| S-EPMC3514462 | biostudies-literature
| S-EPMC4364603 | biostudies-literature
| S-EPMC7098691 | biostudies-literature
| S-EPMC3288512 | biostudies-literature
| S-EPMC3394927 | biostudies-literature