grade
practical grade
mol wt
12327 Da
concentration
≥60% (based on Mol. Wt. 12,327)
UniProt accession no.
storage temp.
−20°C
Gene Information
cow ... CYC1(512500)
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Biochem/physiol Actions
The ready fluctuation of cytochrome c within the cell between ferrous and ferric states, makes it an efficient biological electron-transporter. It plays a vital role in cellular oxidations in both plants and animals. Generally regarded as a universal catalyst of respiration, it forms the essential electron-bridge between the respirable substrates and oxygen.
The ready interconversion of cytochrome c between ferrous and ferric states makes it an efficient biological electron carrier. It plays a vital role in cellular oxidations in both plants and animals. Generally regarded as a universal link in the respiratory chain, it forms the essential electron-bridge between the respirable substrates and oxygen.
Preparation Note
Prepared without using TCA.
Analysis Note
Contains variable amounts of reduced cytochrome c.
Other Notes
View more information on cytochrome c and electron transport at www.sigma-aldrich.com/enzymeexplorer.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Alexander N Volkov et al.
Biochemistry, 52(13), 2165-2175 (2013-03-23)
Here we present the preparation, biophysical characterization, and nuclear magnetic resonance (NMR) spectroscopy study of yeast cytochrome c peroxidase (CcP) constructs with enhanced solubility. Using a high-yield Escherichia coli expression system, we routinely produced uniformly labeled [(2)H,(13)C,(15)N]CcP samples with high
Chris L Bergstrom et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(16), 6269-6274 (2013-04-12)
The release of cytochrome c from mitochondria is a key signaling mechanism in apoptosis. Although extramitochondrial proteins are thought to initiate this release, the exact mechanisms remain unclear. Cytochrome c (cyt c) binds to and penetrates lipid structures containing the
Why is the reduction of NO in cytochrome c dependent nitric oxide reductase (cNOR) not electrogenic?
Margareta R A Blomberg et al.
Biochimica et biophysica acta, 1827(7), 826-833 (2013-04-27)
The membrane-bound enzyme cNOR (cytochrome c dependent nitric oxide reductase) catalyzes the reduction of NO in a non-electrogenic process. This is in contrast to the reduction of O2 in cytochrome c oxidase (CcO), the other member of the heme-copper oxidase
Rawabi Qadhi et al.
Toxicology letters, 219(3), 288-297 (2013-03-26)
The importance of dietary polyunsaturated fatty acids (PUFAs) in the reduction of cardiovascular disease has been recognized for many years. Docosahexaenoic acid (22:6n3, DHA) is an n-3 PUFA known to affect numerous biological functions and provide cardioprotection; however, the exact
Esther Lapuente-Brun et al.
Science (New York, N.Y.), 340(6140), 1567-1570 (2013-07-03)
The textbook description of mitochondrial respiratory complexes (RCs) views them as free-moving entities linked by the mobile carriers coenzyme Q (CoQ) and cytochrome c (cyt c). This model (known as the fluid model) is challenged by the proposal that all
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