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The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics.
Biochemistry. 2006 Mar 14; 45(10):3412-20.B

Abstract

This paper describes the structural and dynamic properties of a hitherto uncovered alkali molten globule (MG) state of horse "ferrocytochrome c" (ferrocyt c). Several experimental difficulties mainly because of heme autoxidation and extraordinary stability of ferrocyt c have been overcome by working with the carbonmonoxide-bound molecule under extremely basic condition (pH 13) in a strictly anaerobic atmosphere. Structural and molecular properties extracted from basic spectroscopic experiments suggest that cations drive the base-denatured CO-liganded protein to the MG state. The stability of this state is approximately 5.2 kcal mol(-)(1), and the guanidinium-induced unfolding transition is sharp (m(g) approximately 2.3 kcal mol(-)(1) M(-)(1)), suggesting contents of rigid tertiary structure. Strategic experiments involving the measurement of the CO association rate to the base-denatured protein and intrachain diffusion rates measured by laser photolysis of CO indicate a substantially restricted overall motion and stiffness of the polypeptide chain in the MG state. Possible placement of the state in the folding coordinate of ferrocyt c is discussed.

Authors+Show Affiliations

Rao DK
School of Chemistry, University of Hyderabad, Hyderabad 500046, India.
Kumar R
No affiliation info available
Yadaiah M
No affiliation info available
Bhuyan AK
No affiliation info available

MeSH

AlkaliesCarbon MonoxideCircular DichroismCytochromes cEnzyme StabilityGuanidineKineticsMolecular ConformationPhotolysisProtein DenaturationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiarySodium ChlorideSpectrophotometry, Ultraviolet

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16519536

Citation

Rao, D Krishna, et al. "The Alkali Molten Globule State of Ferrocytochrome C: Extraordinary Stability, Persistent Structure, and Constrained Overall Dynamics." Biochemistry, vol. 45, no. 10, 2006, pp. 3412-20.
Rao DK, Kumar R, Yadaiah M, et al. The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics. Biochemistry. 2006;45(10):3412-20.
Rao, D. K., Kumar, R., Yadaiah, M., & Bhuyan, A. K. (2006). The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics. Biochemistry, 45(10), 3412-20.
Rao DK, et al. The Alkali Molten Globule State of Ferrocytochrome C: Extraordinary Stability, Persistent Structure, and Constrained Overall Dynamics. Biochemistry. 2006 Mar 14;45(10):3412-20. PubMed PMID: 16519536.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The alkali molten globule state of ferrocytochrome c: extraordinary stability, persistent structure, and constrained overall dynamics. AU - Rao,D Krishna, AU - Kumar,Rajesh, AU - Yadaiah,M, AU - Bhuyan,Abani K, PY - 2006/3/8/pubmed PY - 2006/5/4/medline PY - 2006/3/8/entrez SP - 3412 EP - 20 JF - Biochemistry JO - Biochemistry VL - 45 IS - 10 N2 - This paper describes the structural and dynamic properties of a hitherto uncovered alkali molten globule (MG) state of horse "ferrocytochrome c" (ferrocyt c). Several experimental difficulties mainly because of heme autoxidation and extraordinary stability of ferrocyt c have been overcome by working with the carbonmonoxide-bound molecule under extremely basic condition (pH 13) in a strictly anaerobic atmosphere. Structural and molecular properties extracted from basic spectroscopic experiments suggest that cations drive the base-denatured CO-liganded protein to the MG state. The stability of this state is approximately 5.2 kcal mol(-)(1), and the guanidinium-induced unfolding transition is sharp (m(g) approximately 2.3 kcal mol(-)(1) M(-)(1)), suggesting contents of rigid tertiary structure. Strategic experiments involving the measurement of the CO association rate to the base-denatured protein and intrachain diffusion rates measured by laser photolysis of CO indicate a substantially restricted overall motion and stiffness of the polypeptide chain in the MG state. Possible placement of the state in the folding coordinate of ferrocyt c is discussed. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/16519536/The_alkali_molten_globule_state_of_ferrocytochrome_c:_extraordinary_stability_persistent_structure_and_constrained_overall_dynamics_ DB - PRIME DP - Unbound Medicine ER -