The respiratory chain of mitochondria and bacteria is made up of a set of membrane‐associated enzyme complexes which catalyse sequential, stepwise transfer of reducing equivalents from substrates to oxygen and convert redox energy into a transmembrane protonmotive force (PMF) by proton translocation from a negative (N) to a positive (P) aqueous phase separated by the coupling membrane. There are three basic mechanisms by which a membrane‐associated redox enzyme can generate a PMF. These are membrane anisotropic arrangement of the primary redox catalysis with: (i) vectorial electron transfer by redox metal centres from the P to the N side of the membrane; (ii) hydrogen transfer by movement of quinones across the membrane, from a reduction site at the N side to an oxidation site at the P side; (iii) a different type of mechanism based on co‐operative allosteric linkage between electron transfer at the metal redox centres and transmembrane electrogenic proton translocation by apoproteins.

中文翻译：

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呼吸链酶氧化还原与质子易位的耦合机制

线粒体和细菌的呼吸链由一组膜相关酶复合物组成，这些复合物催化还原当量从底物到氧气的顺序、逐步转移，并通过质子从负离子易位将氧化还原能转化为跨膜质子动力 (PMF)。 (N) 到由耦合膜分离的正 (P) 水相。膜相关氧化还原酶可以通过三种基本机制产生 PMF。这些是初级氧化还原催化的膜各向异性排列，具有： (i) 通过氧化还原金属中心从膜的 P 侧到 N 侧的矢量电子转移；(ii) 通过醌跨膜移动的氢转移，从 N 侧的还原位点到 P 侧的氧化位点；