Electron paramagnetic resonance- (EPR-) resolved kinetics of cryogenic nitric oxide recombination to cytochrome c oxidase and myoglobin

Author:

LoBrutto R.,Wei Y.H.,Yoshida S.,Van Camp H.L.,Scholes C.P.,King T.E.

Publisher

Elsevier BV

Subject

Biophysics

Cited by 16 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Photo-dependent binding structures of CO and NO on the heme-copper site in bovine cytochrome c oxidase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2010-07

2. X-ray structure of the NO-bound CuBin bovine cytochromecoxidase;Acta Crystallographica Section F Structural Biology and Crystallization Communications;2010-02-23

3. The Power of Using Continuous-Wave and Pulsed Electron Paramagnetic Resonance Methods for the Structure Analysis of Ferric Forms and Nitric Oxide-Ligated Ferrous Forms of Globins;Globins and Other Nitric Oxide-Reactive Proteins, Part B;2008

4. 5.2 Nitric Oxide in Regulation of Mitochondrial Function, Respiration, and Glycolysis;Handbook of Neurochemistry and Molecular Neurobiology;2007

5. ENDOR of NO-Ligated Cytochrome c‘;Journal of the American Chemical Society;2006-03-24

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