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Cytochrome c(553), a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics.
J Mol Biol. 2000 Aug 25; 301(4):769-73.JM

Abstract

Cytochrome c(553) (cyt c(553)) from Desulfovibrio vulgaris is a small helical heme protein that displays apparent two-state equilibrium-unfolding behavior. The covalently attached heme is low-spin, ligated by Met and His residues, in the native state but becomes high-spin upon unfolding at pH 7. Here, we show that in contrast to other c-type heme proteins, where misligations in the unfolded states are prominent, cyt c(553) refolding kinetics at pH 7 proceeds rapidly without detectable intermediates. The extrapolated folding rate constant in water for oxidized cyt c(553) matches exactly that predicted from the cyt c(553) native-state topology: 5300 s(-1)(experimental) versus 5020 s(-1) (predicted). We therefore conclude that the presence of the oxidized cofactor does not affect the intrinsic formation speed of the cyt c(553)structural motif.

Authors+Show Affiliations

Chemistry Department, Tulane University, 6823 St. Charles Avenue, New Orleans, LA 70118, USA.No affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

10966783

Citation

Guidry, J, and P Wittung-Stafshede. "Cytochrome C(553), a Small Heme Protein That Lacks Misligation in Its Unfolded State, Folds With Rapid Two-state Kinetics." Journal of Molecular Biology, vol. 301, no. 4, 2000, pp. 769-73.
Guidry J, Wittung-Stafshede P. Cytochrome c(553), a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics. J Mol Biol. 2000;301(4):769-73.
Guidry, J., & Wittung-Stafshede, P. (2000). Cytochrome c(553), a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics. Journal of Molecular Biology, 301(4), 769-73.
Guidry J, Wittung-Stafshede P. Cytochrome C(553), a Small Heme Protein That Lacks Misligation in Its Unfolded State, Folds With Rapid Two-state Kinetics. J Mol Biol. 2000 Aug 25;301(4):769-73. PubMed PMID: 10966783.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cytochrome c(553), a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics. AU - Guidry,J, AU - Wittung-Stafshede,P, PY - 2000/9/1/pubmed PY - 2000/9/23/medline PY - 2000/9/1/entrez SP - 769 EP - 73 JF - Journal of molecular biology JO - J Mol Biol VL - 301 IS - 4 N2 - Cytochrome c(553) (cyt c(553)) from Desulfovibrio vulgaris is a small helical heme protein that displays apparent two-state equilibrium-unfolding behavior. The covalently attached heme is low-spin, ligated by Met and His residues, in the native state but becomes high-spin upon unfolding at pH 7. Here, we show that in contrast to other c-type heme proteins, where misligations in the unfolded states are prominent, cyt c(553) refolding kinetics at pH 7 proceeds rapidly without detectable intermediates. The extrapolated folding rate constant in water for oxidized cyt c(553) matches exactly that predicted from the cyt c(553) native-state topology: 5300 s(-1)(experimental) versus 5020 s(-1) (predicted). We therefore conclude that the presence of the oxidized cofactor does not affect the intrinsic formation speed of the cyt c(553)structural motif. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/10966783/Cytochrome_c_553__a_small_heme_protein_that_lacks_misligation_in_its_unfolded_state_folds_with_rapid_two_state_kinetics_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(00)93993-7 DB - PRIME DP - Unbound Medicine ER -