Oxygen binding and nitric oxide dioxygenase activity of cytoglobin are altered to different extents by cysteine modification

Danlei Zhou; Craig Hemann; James Boslett; Aiqin Luo; Jay L. Zweier; Xiaoping Liu

doi:10.1002/2211-5463.12230

Oxygen binding and nitric oxide dioxygenase activity of cytoglobin are altered to different extents by cysteine modification

Danlei Zhou, Craig Hemann, James Boslett, Aiqin Luo^*, Jay L. Zweier, Xiaoping Liu

^*Corresponding author for this work

School of Life Science

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

Cytoglobin (Cygb), like other members of the globin family, is a nitric oxide (NO) dioxygenase, metabolizing NO in an oxygen (O₂)-dependent manner. We examined the effect of modification of cysteine sulfhydryl groups of Cygb on its O₂ binding and NO dioxygenase activity. The two cysteine sulfhydryls of Cygb were modified to form either an intramolecular disulfide bond (Cygb_SS), thioether bonds to N-ethylmaleimide (NEM; Cygb_SC), or were maintained as free SH groups (Cygb_SH). It was observed that the NO dioxygenase activity of Cygb only slightly changed (~ 25%) while the P₅₀ of O₂ binding to Cygb changed over four-fold with these modifications. Our results suggest that it is possible to separately regulate one Cygb function (such as O₂ binding) without largely affecting the other Cygb functions (such as its NO dioxygenase activity).

Original language	English
Pages (from-to)	845-853
Number of pages	9
Journal	FEBS Open Bio
Volume	7
Issue number	6
DOIs	https://doi.org/10.1002/2211-5463.12230
Publication status	Published - 1 Jun 2017

Keywords

NO dioxygenation
cytoglobin
disulfide bond

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title = "Oxygen binding and nitric oxide dioxygenase activity of cytoglobin are altered to different extents by cysteine modification",

abstract = "Cytoglobin (Cygb), like other members of the globin family, is a nitric oxide (NO) dioxygenase, metabolizing NO in an oxygen (O2)-dependent manner. We examined the effect of modification of cysteine sulfhydryl groups of Cygb on its O2 binding and NO dioxygenase activity. The two cysteine sulfhydryls of Cygb were modified to form either an intramolecular disulfide bond (Cygb_SS), thioether bonds to N-ethylmaleimide (NEM; Cygb_SC), or were maintained as free SH groups (Cygb_SH). It was observed that the NO dioxygenase activity of Cygb only slightly changed (~ 25%) while the P50 of O2 binding to Cygb changed over four-fold with these modifications. Our results suggest that it is possible to separately regulate one Cygb function (such as O2 binding) without largely affecting the other Cygb functions (such as its NO dioxygenase activity).",

keywords = "NO dioxygenation, cytoglobin, disulfide bond",

author = "Danlei Zhou and Craig Hemann and James Boslett and Aiqin Luo and Zweier, {Jay L.} and Xiaoping Liu",

note = "Publisher Copyright: {\textcopyright} 2017 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.",

year = "2017",

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doi = "10.1002/2211-5463.12230",

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TY - JOUR

T1 - Oxygen binding and nitric oxide dioxygenase activity of cytoglobin are altered to different extents by cysteine modification

AU - Zhou, Danlei

AU - Hemann, Craig

AU - Boslett, James

AU - Luo, Aiqin

AU - Zweier, Jay L.

AU - Liu, Xiaoping

PY - 2017/6/1

Y1 - 2017/6/1

N2 - Cytoglobin (Cygb), like other members of the globin family, is a nitric oxide (NO) dioxygenase, metabolizing NO in an oxygen (O2)-dependent manner. We examined the effect of modification of cysteine sulfhydryl groups of Cygb on its O2 binding and NO dioxygenase activity. The two cysteine sulfhydryls of Cygb were modified to form either an intramolecular disulfide bond (Cygb_SS), thioether bonds to N-ethylmaleimide (NEM; Cygb_SC), or were maintained as free SH groups (Cygb_SH). It was observed that the NO dioxygenase activity of Cygb only slightly changed (~ 25%) while the P50 of O2 binding to Cygb changed over four-fold with these modifications. Our results suggest that it is possible to separately regulate one Cygb function (such as O2 binding) without largely affecting the other Cygb functions (such as its NO dioxygenase activity).

AB - Cytoglobin (Cygb), like other members of the globin family, is a nitric oxide (NO) dioxygenase, metabolizing NO in an oxygen (O2)-dependent manner. We examined the effect of modification of cysteine sulfhydryl groups of Cygb on its O2 binding and NO dioxygenase activity. The two cysteine sulfhydryls of Cygb were modified to form either an intramolecular disulfide bond (Cygb_SS), thioether bonds to N-ethylmaleimide (NEM; Cygb_SC), or were maintained as free SH groups (Cygb_SH). It was observed that the NO dioxygenase activity of Cygb only slightly changed (~ 25%) while the P50 of O2 binding to Cygb changed over four-fold with these modifications. Our results suggest that it is possible to separately regulate one Cygb function (such as O2 binding) without largely affecting the other Cygb functions (such as its NO dioxygenase activity).

KW - NO dioxygenation

KW - cytoglobin

KW - disulfide bond

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U2 - 10.1002/2211-5463.12230

DO - 10.1002/2211-5463.12230

M3 - Article

AN - SCOPUS:85019921847

SN - 2211-5463

VL - 7

SP - 845

EP - 853

JO - FEBS Open Bio

JF - FEBS Open Bio

IS - 6

ER -

Oxygen binding and nitric oxide dioxygenase activity of cytoglobin are altered to different extents by cysteine modification

Abstract

Keywords

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