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Article

Electronic control of discrimination between O2 and CO in myoglobin lacking the distal histidine residue.

Inorganic chemistry - 21 Jan 2014

Nishimura Ryu, Shibata Tomokazu, Ishigami Izumi, Ogura Takashi, Tai Hulin, Nagao Satoshi, Matsuo Takashi, Hirota Shun, Shoji Osami, Watanabe Yoshihito, Imai Kiyohiro, Neya Saburo, Suzuki Akihiro, Yamamoto Yasuhiko

Abstract excerpt

We analyzed the oxygen (O2) and carbon monoxide (CO) binding properties of the H64L mutant of myoglobin reconstituted with chemically modified heme cofactors possessing a heme Fe atom with a variety of electron densities, in order to elucidate the effect of the removal of the distal His64 on the control of both the O2 affinity and discrimination between O2 and CO of the protein by the intrinsic heme Fe reactivity...

Topics

Animals
Carbon Monoxide
Electrons
Heme
Histidine
Mutant Proteins
Mutation
Myoglobin
Oxygen
Substrate Specificity
Vibration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 24377722
DOI: 10.1021/ic402625s

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