Local Stability of Rhodobacter capsulatus Cytochrome c2 Probed by Solution Phase Hydrogen/Deuterium Exchange and Mass Spectrometry

Journal of the American Society for Mass Spectrometry

Volumn 17, Issue 11, 2006, Pages 1518-1525

  Cheng, Guilong ^a   Wysocki, Vicki H ^a   Cusanovich, Michael A ^b  

^a University of Arizona   (United States)

^b UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; HYDROGEN; HYDROGEN BONDS; MASS SPECTROMETRY; OXIDATION; PROTEINS;

DESTABILIZATION; DEUTERIUM EXCHANGE; RELATIVE DOMAIN STABILITY; RHODOBACTER CAPSULATUS CYTOCHROME;

CYTOLOGY;

AMINO ACID; BACTERIAL PROTEIN; CYTOCHROME C2; DEUTERIUM; HEME; HYDROGEN; HYDROXYL GROUP; LYSINE; METHIONINE; PROLINE; PROPIONIC ACID;

ARTICLE; DEUTERIUM HYDROGEN EXCHANGE; HYDROGEN BOND; LIGAND BINDING; MASS SPECTROMETRY; NONHUMAN; OXIDATION; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; RHODOBACTER CAPSULATUS; STRUCTURAL HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; CYTOCHROMES C2; DEUTERIUM EXCHANGE MEASUREMENT; HORSES; HYDROGEN; MOLECULAR SEQUENCE DATA; PEPTIDE MAPPING; RHODOBACTER CAPSULATUS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EQUUS CABALLUS; RHODOBACTER CAPSULATUS;

EID: 33750296444     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2006.04.028     Document Type: Article

References (15)

1. Bai Y., Sosnick T.R., Mayne L., and Englander S.W. Protein folding intermediates: Native-state hydrogen exchange. Science 269 5221 (1995) 192-197
2. Hoang L., Maity H., Krishna M.M.G., Lin Y., and Englander S.W. Folding units govern the cytochrome c alkaline transition. J. Mol. Biol. 331 1 (2003) 37-43
3. Krishna Mallela M.G., Lin Y., Mayne L., and Englander S.W. Intimate view of a kinetic protein folding intermediate: residue-resolved structure, interactions, stability, folding, and unfolding rates, homogeneity. J. Mol. Biol. 334 3 (2003) 501-513
4. Zhang Z., and Smith D.L. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci. 2 4 (1993) 522-531
5. Dharmasiri K., and Smith D.L. Regional stability changes in oxidized and reduced cytochrome c located by hydrogen exchange and mass spectrometry. J. Am. Soc. Mass Spectrom. 8 10 (1997) 1039-1045
6. Englander J.J., Del Mar C., Li W., Englander S.W., Kim J.S., Stranz D.D., Hamuro Y., and Woods Jr. V.L. Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 100 12 (2003) 7057-7062
7. 2 isolated from Rhodobacter capsulatus determined at 2.5. ANG. resolution. J. Mol. Biol. 220 3 (1991) 673-685
8. Meyer T.E., and Cusanovich M.A. Discovery and characterization of electron transfer proteins in the photosynthetic bacteria. Photosynth. Res. 76 1/3 (2003) 111-126
9. 2 hinge mutants. Biochemistry 43 24 (2004) 7717-7724
10. 2 to photosynthetic reaction centers: Plasmon-waveguide resonance spectroscopy. Biochemistry 43 51 (2004) 16405-16415
11. Caffrey M.S., and Cusanovich M.A. Site-specific mutagenesis studies of cytochromes c. Biochim. Biophys. Acta 1187 3 (1994) 277-288
12. Englander J.J., Rogero J.R., and Englander S.W. Protein hydrogen exchange studied by the fragment separation method. Anal. Biochem. 147 1 (1985) 234-244
13. Zhang Z., and Marshall A.G. A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra. J. Am. Soc. Mass Spectrom. 9 3 (1998) 225-233
14. 2. Protein Sci. 9 9 (2000) 1828-1837
15. Blouin C., and Wallace C.J.A. Protein matrix and dielectric effect in cytochrome c. J. Biol. Chem. 276 31 (2001) 28814-28818