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Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH‐dependent scavenging of nitric oxide
Author(s) -
Igamberdiev Abir U,
Bykova Natalia V,
Ens Werner,
Hill Robert D
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.05.024
Subject(s) - dihydrolipoamide dehydrogenase , chemistry , methemoglobin , diaphorase , electron acceptor , myoglobin , nitrite , nitric oxide , dehydrogenase , photochemistry , electron donor , reductase , methylene blue , nadh dehydrogenase , enzyme , cyanide , biochemistry , nitrate , hemoglobin , inorganic chemistry , catalysis , organic chemistry , photocatalysis , protein subunit , gene
Dihydrolipoamide dehydrogenase (DLDH; EC 1.8.1.4) from porcine heart is capable of using nitric oxide (NO) as an electron acceptor, with NADH as the electron donor, forming nitrate in the reaction. NADPH was not effective as an electron donor. The reaction had a pH optimum near 6 and was not inhibited by cyanide or diphenyleneiodonium ions. The K m for NADH was 10 μM, while that for NO was 0.5 μM. The rate of NO conversion was comparable to the rate of lipoamide conversion (200 μmol min −1 mg −1 protein at pH 6). Cytochrome c or myoglobin were poor electron acceptors by themselves but, in the presence of methylene blue, DLDH had an activity of 5–7 μmol min −1 mg −1 protein with these substrates, indicating that DLDH can act also as a methemoglobin reductase. While the K m of DLDH for NO is relatively low, it is in the physiological range of NO levels encountered in the tissue. The enzyme may, therefore, have a significant role in modifying NO levels under specific cell conditions.