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Cytochrome c' of Methylococcus capsulatus Bath
J A Zahn1, D M Arciero, A B Hooper
1Department of Microbiology, Immunology, and Preventive Medicine, Iowa State University, Iowa 50011-3211, USA.
European Journal of Biochemistry
|September 15, 1996
Summary
Researchers isolated cytochrome c
Area of Science:
- Biochemistry
- Microbiology
Background:
- Methylococcus capsulatus Bath is an obligate methylotroph.
- Cytochromes c' are heme-containing proteins involved in electron transport.
Purpose of the Study:
- To characterize cytochrome c' from Methylococcus capsulatus Bath.
- To investigate its ligand binding properties and redox behavior.
Main Methods:
- Isolation and purification of cytochrome c'.
- Spectroscopic analysis (EPR, optical absorption).
- Analytical ultracentrifugation.
- Midpoint potential determination.
Main Results:
- Cytochrome c' from M. capsulatus Bath has a native molecular mass of 34.9 kDa and subunit mass of 16.2 kDa.
- It binds carbon monoxide and nitric oxide, undergoing conformational changes, not dimer dissociation.
- Its midpoint potential (Em 7.0 = -250 mV) suggests a role as an electron shuttle.
Conclusions:
- Cytochrome c' from M. capsulatus Bath exhibits unique properties compared to other cytochromes c'.
- Its low midpoint potential indicates a specific role in the electron transport chain, potentially linking cytochrome P-460 and cytochrome C555.