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Topic: Cytochrome C

Related Topics

Electron transport

Cytochrome

Cytochrome c peroxidase

Leghemoglobin

Heme

Cytochrome c oxidase

Hemoglobin

Myoglobin

Ferryl

Azide

Oxidation

Cyanide

Potassium cyanide

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	Cytochrome
		The fluorescence spectra of the molybdenum cofactor derivative prepared from cytochrome a1c1 were very similar to those of the cofactor derivative from xanthine oxidase, and the aponitrate reductase of nit-1 mutant of Neurospora crassa was complemented by addition of the molybdenum cofactor derived from the cytochrome.
		Further, the ESR spectrum of cytochrome a1c1 was similar to that of liver sulfite oxidase.
		The content of cytochrome a1 in the cells cultivated with the medium in which tungsten was substituted for molybdenum markedly decreased as compared with that in the cells cultivated in the molybdenum-supplemented medium.
	www.ithyroid.com /cytochrome.htm (1736 words)

	29+ Evidences for Macroevolution: Part 4
		Cytochrome c is an essential and ubiquitous protein found in all organisms, including eukaryotes and bacteria (Voet and Voet 1995, p.
		Finally, the similarity observed for cytochrome c is not confined to this single ubiquitous protein; all ubiquitous proteins that have been compared between chimpanzees and humans are highly similar, and there have been many comparisons.
		Yandava, C. N., Gastier, J. M., Pulido, J. C., Brody, T., Sheffield, V., Murray, J., Buetow, K., and Duyk, G. (1997) "Characterization of Alu repeats that are associated with trinucleotide and tetranucleotide repeat microsatellites." Genome Res.
	www.talkorigins.org /faqs/comdesc/section4.html (5370 words)

	Cytochromes c
		The haem c groups, all bisHis coordinated, are structurally and functionally nonequivalent and present different redox potentials in the range 0 to -400 mV [5].
		Alternatively, Moore and Pettigrew [2] have suggested that Class IV cyt c are tetrahaem proteins containing both bisHis and HisMet coordinated haems, with a 3D structure exemplified by that of the photosynthetic reaction centre (PRC) cyt c, and form a structurally homogeneous family.
		Fülöp, V., Ridout, C.J., Greenwood, C. and Hajdu, J. Crystal structure of the dihaem cytochrome c peroxidase from Pseudomonas aeruginosa.
	metallo.scripps.edu /PROMISE/CYTC.html (678 words)

	Cytochrome c oxidase at opensource encyclopedia (Site not responding. Last check: 2007-10-09)
		The enzyme cytochrome c oxidase (PDB 2OCC, EC 1.9.3.1) is a large transmembrane protein found in the mitochondrion and is the terminal electron acceptor in the electron transfer chain, taking 4 reducing equivalents from cytochrome c and converting molecular oxygen to water.
		The complex contains 2 cytochromes, the a and a
		cytochromes, and two copper centers, the Cu and Cu centers.
	www.wiki.tatet.com /Cytochrome_c_oxidase.html (171 words)

	Cytochrome P-450 (Site not responding. Last check: 2007-10-09)
		The term CYTOCHROME P-450 refers to a group of enzymes with are located on the endoplasmic reticulum.
		It is know that the gene for cytochrome P-450 has existed for more then 3.5 billion years.
		The second table shows various drugs and the various cytochrome P-450 enzyme systems that either inhibit or induce that drugs metabolism.
	www.edhayes.com /startp450.html (323 words)

	Ameeta Kelekar, Ph.D.
		Pro-apoptotic members of the family promote the release of mitochondrial cytochrome c and cause cell death, while anti-apoptotic proteins prevent its release allowing cells to survive.
		Caspase-9 is activated in a cytochrome c-independent manner early during TNFa-induced apoptosis in murine cells.
		Cytochrome c is released in a single step during apoptosis.
	www.mimp.umn.edu /faculty/Kelekar.html (722 words)

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