☆ 4.6 Article

Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2008)

期刊

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

卷 367, 期 4, 页码 852-858

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE

DOI: 10.1016/j.bbrc.2008.01.016

关键词

heme oxygenase; NADPH-cytochrome P450 reductase; biliverdin reductase; MALDI-TOF mass spectrometry; chemical modification; protein-protein interaction

类别

Biochemistry & Molecular Biology Biophysics

资金

NIGMS NIH HHS [R01 GM080575-01, R01 GM080575, GM 080575] Funding Source: Medline

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摘要

The lysine residues of rat heme oxygenase-1 (HO-1) were acetylated by acetic anhydride in the absence and presence of NADPH-cytochrome P450 reductase (CPR) or biliverdin reductase (BVR). Nine acetylated peptides were identified by MALDI-TOF mass spectrometry in the tryptic fragments obtained from HO-1 acetylated without the reductases (referred to as the fully acetylated HO-1). The presence of CPR prevented HO-1 from acetylation of lysine residues, Lys-149 and Lys-153, located in the F-helix. The heme degradation activity of the fully acetylated HO-1 in the NADPH/CPR-supported system was significantly reduced, whereas almost no inactivation was detected in HO-1 in the presence of CPR, which prevented acetylation of Lys-149 and Lys-153. On the other hand, the presence of BVR showed no protective effect on the acetylation of HO-1. The interaction of HO-1 with CPR or BVR is discussed based on the acetylation pattern and on molecular modeling. (c) 2008 Elsevier Inc. All rights reserved.

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