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The off-pathway status of the alkali molten globule is unrelated to heme misligation and trans-pH effects: experiments with ferrocytochrome c.
Biochemistry. 2010 Sep 14; 49(36):7774-82.B

Abstract

The relevance of the alkali molten globule (B-state) to the folding pathway of cytochrome c has been studied further with the reduced state of the protein for which the B-state is prepared by ligating the ferrous heme iron with extrinsic CO under 1 mM gas concentration in the presence of NaCl. The CO derivative of ferrocytochrome c is desirable not only because it abrogates the interference of non-native heme ligands but the GdnHCl-unfolded protein refolds fast without deviating from the intrinsic folding pathway of the protein. Interstate folding-unfolding kinetics at alkaline and neutral pH conditions reveal that the B-state chain initially expands in the submillisecond regime in order to fold correctly to the native state. In this sense, it is an off-pathway nonproductive species which must dissipate some non-native elements before proceeding to fold. It is concluded that the alkali molten globule does not correspond to any possible transient structure in the folding pathway of cytochrome c.

Authors+Show Affiliations

School of Chemistry, University of Hyderabad, Hyderabad 500046, India. akbsc@uohyd.ernet.in

Pub Type(s)

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

Language

eng

PubMed ID

20687524

Citation

Bhuyan, Abani K.. "The Off-pathway Status of the Alkali Molten Globule Is Unrelated to Heme Misligation and trans-pH Effects: Experiments With Ferrocytochrome C." Biochemistry, vol. 49, no. 36, 2010, pp. 7774-82.
Bhuyan AK. The off-pathway status of the alkali molten globule is unrelated to heme misligation and trans-pH effects: experiments with ferrocytochrome c. Biochemistry. 2010;49(36):7774-82.
Bhuyan, A. K. (2010). The off-pathway status of the alkali molten globule is unrelated to heme misligation and trans-pH effects: experiments with ferrocytochrome c. Biochemistry, 49(36), 7774-82. https://doi.org/10.1021/bi100881n
Bhuyan AK. The Off-pathway Status of the Alkali Molten Globule Is Unrelated to Heme Misligation and trans-pH Effects: Experiments With Ferrocytochrome C. Biochemistry. 2010 Sep 14;49(36):7774-82. PubMed PMID: 20687524.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The off-pathway status of the alkali molten globule is unrelated to heme misligation and trans-pH effects: experiments with ferrocytochrome c. A1 - Bhuyan,Abani K, PY - 2010/8/7/entrez PY - 2010/8/7/pubmed PY - 2010/11/4/medline SP - 7774 EP - 82 JF - Biochemistry JO - Biochemistry VL - 49 IS - 36 N2 - The relevance of the alkali molten globule (B-state) to the folding pathway of cytochrome c has been studied further with the reduced state of the protein for which the B-state is prepared by ligating the ferrous heme iron with extrinsic CO under 1 mM gas concentration in the presence of NaCl. The CO derivative of ferrocytochrome c is desirable not only because it abrogates the interference of non-native heme ligands but the GdnHCl-unfolded protein refolds fast without deviating from the intrinsic folding pathway of the protein. Interstate folding-unfolding kinetics at alkaline and neutral pH conditions reveal that the B-state chain initially expands in the submillisecond regime in order to fold correctly to the native state. In this sense, it is an off-pathway nonproductive species which must dissipate some non-native elements before proceeding to fold. It is concluded that the alkali molten globule does not correspond to any possible transient structure in the folding pathway of cytochrome c. SN - 1520-4995 UR - https://www.unboundmedicine.com/medline/citation/20687524/The_off_pathway_status_of_the_alkali_molten_globule_is_unrelated_to_heme_misligation_and_trans_pH_effects:_experiments_with_ferrocytochrome_c_ L2 - https://doi.org/10.1021/bi100881n DB - PRIME DP - Unbound Medicine ER -
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