期刊
ISRAEL JOURNAL OF CHEMISTRY
卷 56, 期 9-10, 页码 693-704出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/ijch.201600021
关键词
electronic coupling; electron transfer; heme ruffling; hydrogen bonds; hyperfine shift
资金
- Chemical Sciences, Geosciences and Biosciences Division, Office of Basic Energy Sciences, Office of Science, U.S. Department of Energy [DE-FG02-09ER16121]
- National Science Foundation [CHE-1409929]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1409929] Funding Source: National Science Foundation
Heme is an essential and functionally versatile cofactor. Our understanding of how the environment of a heme in a protein tunes its function has benefited from spectroscopic and functional investigations of heme proteins and their variants with altered heme environments. Two properties of current interest are the conformation of the heme and hydrogen bonding to heme propionates. By combining nuclear magnetic resonance experiments and density functional theory calculations, both of these characteristics have been shown to influence the distribution of the singly occupied molecular orbital on the heme of ferricytochrome c, which affects coupling to redox partners and electron-transfer rates. In addition, heme conformation has been shown to tune reduction potential. These results reveal that subtle variations in heme conformation and in interactions with its propionates can have significant impacts on electron-transfer activity.
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