期刊
COORDINATION CHEMISTRY REVIEWS
卷 257, 期 2, 页码 511-527出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.ccr.2012.05.008
关键词
Carbon monoxide; Dioxygen; Nitric oxide; Heme; Protein; Raman; Infrared; DFT; Backbonding
资金
- NIH [GM33576]
The gaseous XO molecules (X = C, N or O) bind to the heme prosthetic group of heme proteins, and thereby activate or inhibit key biological processes. These events depend on interactions of the surrounding protein with the FeXO adduct, interactions that can be monitored via the frequencies of the Fe X and X-O bond stretching modes, nu FeX and nu XO. The frequencies can be determined by vibrational spectroscopy, especially resonance Raman spectroscopy. Backbonding, the donation of Fe d(pi) electrons to the XO pi* orbitals, is a major bonding feature in all the FeXO adducts. Variations in backbonding produce negative nu FeX/nu XO correlations, which can be used to gauge electrostatic and H-bonding effects in the protein binding pocket. Backbonding correlations have been established for all the FeXO adducts, using porphyrins with electron donating and withdrawing substituents. However the adducts differ in their response to variations in the nature of the axial ligand, and to specific distal interactions. These variations provide differing vantages for evaluating the nature of protein-heme interactions. We review experimental studies that explore these variations, and DFT computational studies that illuminate the underlying physical mechanisms. Published by Elsevier B.V.
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