TY - JOUR
T1 - Responses of the Fe(CN)2(CO) unit to electronic changes as related to its role in [NiFe]hydrogenase
AU - Lai, Chia Huei
AU - Lee, Way Zen
AU - Miller, Matthew L.
AU - Reibenspies, Joseph H.
AU - Darensbourg, Donald J.
AU - Darensbourg, Marcetta Y.
PY - 1998/10/7
Y1 - 1998/10/7
N2 - The observation of nearly identical infrared spectra in the diatomic (2000 cm-1) region of oxidized forms of [NiFe]hydrogenases, as isolated from Chromatium vinosum (Happe et al. Nature 1997, 385, 126) and Desulfovibrio gigas (Volbeda et al. J. Am. Chem. Soc. 1996, 118, 12989) and the anion (η5-C5H5)Fe-(CN)2(CO)- (Darensbourg et al. J. Am. Chem. Soc. 1997, 119, 7903), including isotopic label shifts, has prompted further development of the organometallic model complex as a spectroscopic reference. The vibrational spectroscopy of the pyramidal Fe(CN)2(CO) unit found in the salts of (η5-C5H5)Fe(CN)2(CO)- and (η5-C5Me5)Fe(CN)2(CO)- is thoroughly investigated with respect to band positions and intensity ratios as influenced by counterion and solvent. The neutral analogues (η5- C5H5)- and (η5-C5Me5)Fe(CN)(CO)2 as well as the protonated H[(η5=- C5H5)Fe(CN)2(CO)] are included for comparison. The X-ray crystal structure of the latter finds short interionic N····N distances of 2.55 Å indicative of CN-nitrogen protonation and strong H-bonding as similarly seen in the attachment of Fe(CN)2(CO) to the protein found in the crystal structure of [NiFe]H2-ase enzyme isolated from the D. gigas bacteria. For a series of nine complexes that covers a broad range of electronic effects (as confirmed by electrochemical studies) within a constant hexacoordinate structure and medium (CH3CN), there is an excellent linearity in the correlation between v(CO) (or F(CO)) and v(CN) (or F(CN)). The enzyme states that are not in the catalytic cycle reasonably fit the model complex correlation and are expected to maintain hexacoordination about iron. The possible source(s) of deviations from this correlation both in the model (in aqueous media) and in the enzyme system are discussed.
AB - The observation of nearly identical infrared spectra in the diatomic (2000 cm-1) region of oxidized forms of [NiFe]hydrogenases, as isolated from Chromatium vinosum (Happe et al. Nature 1997, 385, 126) and Desulfovibrio gigas (Volbeda et al. J. Am. Chem. Soc. 1996, 118, 12989) and the anion (η5-C5H5)Fe-(CN)2(CO)- (Darensbourg et al. J. Am. Chem. Soc. 1997, 119, 7903), including isotopic label shifts, has prompted further development of the organometallic model complex as a spectroscopic reference. The vibrational spectroscopy of the pyramidal Fe(CN)2(CO) unit found in the salts of (η5-C5H5)Fe(CN)2(CO)- and (η5-C5Me5)Fe(CN)2(CO)- is thoroughly investigated with respect to band positions and intensity ratios as influenced by counterion and solvent. The neutral analogues (η5- C5H5)- and (η5-C5Me5)Fe(CN)(CO)2 as well as the protonated H[(η5=- C5H5)Fe(CN)2(CO)] are included for comparison. The X-ray crystal structure of the latter finds short interionic N····N distances of 2.55 Å indicative of CN-nitrogen protonation and strong H-bonding as similarly seen in the attachment of Fe(CN)2(CO) to the protein found in the crystal structure of [NiFe]H2-ase enzyme isolated from the D. gigas bacteria. For a series of nine complexes that covers a broad range of electronic effects (as confirmed by electrochemical studies) within a constant hexacoordinate structure and medium (CH3CN), there is an excellent linearity in the correlation between v(CO) (or F(CO)) and v(CN) (or F(CN)). The enzyme states that are not in the catalytic cycle reasonably fit the model complex correlation and are expected to maintain hexacoordination about iron. The possible source(s) of deviations from this correlation both in the model (in aqueous media) and in the enzyme system are discussed.
UR - http://www.scopus.com/inward/record.url?scp=0032494399&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032494399&partnerID=8YFLogxK
U2 - 10.1021/ja982053a
DO - 10.1021/ja982053a
M3 - Article
AN - SCOPUS:0032494399
SN - 0002-7863
VL - 120
SP - 10103
EP - 10114
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 39
ER -