ATP induces conformational changes in mitochondrial cytochrome c oxidase. Effect on the cytochrome c binding site.
نویسندگان
چکیده
منابع مشابه
The cytochrome c binding site on cytochrome c oxidase.
Cytochrome c oxidase (EC 1.9.3.1) is the terminal enzyme of the mitochondria respiratory chain catalysing electron transfer from cytochrome c to molecular oxygen [ 1,2]. The molecular mechanism of this process is still not understood. At present, little is known about such important structural features as the position of the prosthetic groups or the location and characteristics of the cytochrom...
متن کاملATP induces a conformational change in lipid-bound cytochrome c.
Resonance energy transfer studies using a pyrene-labeled phospholipid derivative 1-palmitoyl-2-[10-(pyren-1-yl)decanoyl]-sn-glycero-3-phosphoglycerol (donor) and the heme (acceptor) of cytochrome c (cyt c) have indicated that ATP causes changes in the conformation of the lipid-bound protein (Rytömaa, M., Mustonen, P., and Kinnunen, P. K. J. (1992) J. Biol. Chem. 267, 22243-22248). Accordingly, ...
متن کاملEFFECT OF CROSSLINKING ON MITOCHONDRIAL CYTOCHROME c OXIDASE
Purified and reconstituted cytpchrome ~oxidase and mitochondria were crosslinked with biimidates in the presence and absence of cytochrome c. These experiments indicate that oxidase subunit interactions are required for activity and that cytochrome~ mobility may be required for electron transport activity. Biimidate treatment of purified and reconstituted oxidase crosslinks all of the oxidase p...
متن کاملRapid electrostatic evolution at the binding site for cytochrome c on cytochrome c oxidase in anthropoid primates.
Cytochrome c (CYC) oxidase (COX), a multisubunit enzyme that functions in mitochondrial aerobic energy production, catalyzes the transfer of electrons from CYC to oxygen and participates in creating the electrochemical gradient used for ATP synthesis. Modeling three-dimensional structural data on COX and CYC reveals that 57 of the >1,500 COX residues can be implicated in binding CYC. Because of...
متن کاملConformational changes in cytochrome c and cytochrome oxidase upon complex formation: a resonance Raman study.
The fully oxidized complex of cytochrome c and cytochrome oxidase formed at low ionic strength was studied by resonance Raman spectroscopy. The spectra of the complex and of the individual components were compared over a wide frequency range using Soret band excitation. In both partners of the complex, structural changes occur in the heme groups and in their immediate protein environment. The s...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)45527-5