FEBS Letters | |
Nitric oxide synthase activity in mitochondria | |
Ghafourifar, Pedram1  Richter, Christoph1  | |
[1] Laboratory of Biochemistry I, Swiss Federal Institute of Technology (ETH), 8092 Zurich, Switzerland | |
关键词: Nitric oxide; Mitochondrial respiration; Mitochondrial membrane potential; BM; broken mitochondria; ΔΨ; mitochondrial membrane potential; IM; intact mitochondria; l-NMMA; N ω-monomethyl-l-arginine; metHb; methemoglobin; mtNOS; mitochondrial nitric oxide synthase; MP; mitoplast; NO; nitric oxide (synonym nitrogen monoxide); l-NA; N ω-nitro-l-arginine; NOS; nitric oxide synthase; HbO2; oxyhemoglobin; SMP; submitochondrial particles; SOD; superoxide dismutase; | |
DOI : 10.1016/S0014-5793(97)01397-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
In the present study we show the existence of a functional nitric oxide synthase (NOS) in rat liver mitochondria. The enzyme uses l-arginine (l-arg) to produce nitric oxide (NO) and l-citrulline, and is Ca2+-dependent. l-Arg analogues, N ω-monomethyl-l-arg and N ω-nitro-l-arg, inhibit the enzyme, and d-arginine is not a substrate for it. We found mitochondrial NOS (mtNOS) activity associated with the inner mitochondrial membrane but not with the matrix fraction. In intact, succinate-energized mitochondria, the enzyme is constitutively active and exerts substantial control over mitochondrial respiration and membrane potential. The activity is further stimulated when Ca2+ is taken up by mitochondria. We suggest that the existence of mtNOS and its Ca2+ dependence are highly relevant for mitochondrial functioning.
【 授权许可】
Unknown
【 预 览 】
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