Potentiometric study of cytochrome c1aa3 from thermus thermophilus
dc.contributor.author | Yoshida, Tatsuro | en_US |
dc.contributor.author | Fee, James A. | en_US |
dc.date.accessioned | 2006-04-07T19:08:47Z | |
dc.date.available | 2006-04-07T19:08:47Z | |
dc.date.issued | 1985 | en_US |
dc.identifier.citation | Yoshida, Tatsuro, Fee, James A. (1985)."Potentiometric study of cytochrome c1aa3 from thermus thermophilus." Journal of Inorganic Biochemistry 23(3-4): 279-288. <http://hdl.handle.net/2027.42/25750> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6TGG-42SR1HS-B5/2/791e025ba5dc4b93b4098bd4de326135 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/25750 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2991468&dopt=citation | en_US |
dc.description.abstract | We have examined the redox behavior of the cytochrome c1aa3 complex from Thermus thermophilus. In potentiometric titrations the cytochrome c behaves as an independent center having n = 1 and E = 205 mV (NHE). Under the assumption that the individual centers equilibrate independently in this experiment, changes in the absorption band at 603 nm have been resolved into two components: cytochrome a (n = 1, Em = 270 mV, 60% spectral contribution) and cytochrome a3 (n = 2, Em= 360 mV, 40% spectral contribution). The n = 2 process was attributed to strong chemical coupling between cytochrome a3 and CuB. The enzyme was also titrated with a mixture of NADH and PMS, and the results are shown not to conform to a model of intramolecular equilibrium according to the equilibrium constants obtained from the potentiometric titration. It is suggested that a conformational equilibrium within the complex may control electron transfer between cytochromes a and a3. | en_US |
dc.format.extent | 625485 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Potentiometric study of cytochrome c1aa3 from thermus thermophilus | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Biophysics Research Division and the Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan U.S.A. | en_US |
dc.contributor.affiliationum | Biophysics Research Division and the Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan U.S.A. | en_US |
dc.identifier.pmid | 2991468 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/25750/1/0000310.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0162-0134(85)85036-4 | en_US |
dc.identifier.source | Journal of Inorganic Biochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.