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

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

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

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 through the electron density of the heme Fe atom (ρFe). The study revealed that, as in the case of the native protein, the O2 affinity of the H64L mutant protein is regulated by the ρFe value in such a manner that the O2 affinity of the protein decreases, due to an increase in the O2 dissociation rate constant, with a decrease in the ρFe value, and that the O2 affinities of the mutant and native proteins are affected comparably by a given change in the ρFe value. On the other hand, the CO affinity of the H64L mutant protein was found to increase, due to a decrease in the CO dissociation rate constant, with a decrease in the ρFe value, whereas that of the native protein was essentially independent of a change in the ρFe value. As a result, the regulation of the O2/CO discrimination in the protein through the ρFe value is affected by the distal His64. Thus, the study revealed that the electronic tuning of the intrinsic heme Fe reactivity through the ρFe value plays a vital role in the regulation of the protein function, as the heme environment furnished by the distal His64 does.

Original languageEnglish (US)
Pages (from-to)1091-1099
Number of pages9
JournalInorganic Chemistry
Volume53
Issue number2
DOIs
StatePublished - Jan 21 2014
Externally publishedYes

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electronic control
myoglobin
histidine
Myoglobin
Carbon Monoxide
Heme
Histidine
carbon monoxide
discrimination
proteins
Mutant Proteins
affinity
Proteins
Carrier concentration
Rate constants
Atoms
reactivity
dissociation
Tuning
Oxygen

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry

Cite this

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

In: Inorganic Chemistry, Vol. 53, No. 2, 21.01.2014, p. 1091-1099.

Research output: Contribution to journalArticle

Nishimura, R, Shibata, T, Ishigami, I, Ogura, T, Tai, H, Nagao, S, Matsuo, T, Hirota, S, Shoji, O, Watanabe, Y, Imai, K, Neya, S, Suzuki, A & Yamamoto, Y 2014, 'Electronic control of discrimination between O2 and CO in myoglobin lacking the distal histidine residue', Inorganic Chemistry, vol. 53, no. 2, pp. 1091-1099. https://doi.org/10.1021/ic402625s
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. / Electronic control of discrimination between O2 and CO in myoglobin lacking the distal histidine residue. In: Inorganic Chemistry. 2014 ; Vol. 53, No. 2. pp. 1091-1099.
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AU - Nishimura, Ryu

AU - Shibata, Tomokazu

AU - Ishigami, Izumi

AU - Ogura, Takashi

AU - Tai, Hulin

AU - Nagao, Satoshi

AU - Matsuo, Takashi

AU - Hirota, Shun

AU - Shoji, Osami

AU - Watanabe, Yoshihito

AU - Imai, Kiyohiro

AU - Neya, Saburo

AU - Suzuki, Akihiro

AU - Yamamoto, Yasuhiko

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N2 - 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 through the electron density of the heme Fe atom (ρFe). The study revealed that, as in the case of the native protein, the O2 affinity of the H64L mutant protein is regulated by the ρFe value in such a manner that the O2 affinity of the protein decreases, due to an increase in the O2 dissociation rate constant, with a decrease in the ρFe value, and that the O2 affinities of the mutant and native proteins are affected comparably by a given change in the ρFe value. On the other hand, the CO affinity of the H64L mutant protein was found to increase, due to a decrease in the CO dissociation rate constant, with a decrease in the ρFe value, whereas that of the native protein was essentially independent of a change in the ρFe value. As a result, the regulation of the O2/CO discrimination in the protein through the ρFe value is affected by the distal His64. Thus, the study revealed that the electronic tuning of the intrinsic heme Fe reactivity through the ρFe value plays a vital role in the regulation of the protein function, as the heme environment furnished by the distal His64 does.

AB - 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 through the electron density of the heme Fe atom (ρFe). The study revealed that, as in the case of the native protein, the O2 affinity of the H64L mutant protein is regulated by the ρFe value in such a manner that the O2 affinity of the protein decreases, due to an increase in the O2 dissociation rate constant, with a decrease in the ρFe value, and that the O2 affinities of the mutant and native proteins are affected comparably by a given change in the ρFe value. On the other hand, the CO affinity of the H64L mutant protein was found to increase, due to a decrease in the CO dissociation rate constant, with a decrease in the ρFe value, whereas that of the native protein was essentially independent of a change in the ρFe value. As a result, the regulation of the O2/CO discrimination in the protein through the ρFe value is affected by the distal His64. Thus, the study revealed that the electronic tuning of the intrinsic heme Fe reactivity through the ρFe value plays a vital role in the regulation of the protein function, as the heme environment furnished by the distal His64 does.

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