Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C.
Abstract: Time-resolved spectroscopic studies of unfolded horse iron(II) cytochrome c have suggested that the imidazole side chains of His26 and His33 bind transiently to the heme iron on microsecond time scales, after photodissociation of a carbon monoxide ligand from the heme. Our studies of four variants of cytochrome c (horse wild type, horse H33N, horse H33N/H26Q, and tuna wild type), unfolded in guanidine hydrochloride at pH 6.5, demonstrate that these side chains are responsible for the observed microsecond spectral changes. As His33 and then His26 are eliminated from the horse wild-type sequence, transient optical absorption spectra show systematic suppression of a rapid (approximately 10-100 micros) Soret absorbance change that follows photolysis of CO. Transient binding of these histidine side chains to the heme therefore generates one of the fast kinetic phases observed in previous photochemically triggered spectroscopic studies of dynamics in unfolded iron(II) cytochrome c. Furthermore, both His33 and His26 appear to contribute to a similar extent in these early kinetics. Thus, the stiffness of the polypeptide chain creates a deviation from Gaussian chain behavior by impeding, although not preventing, the formation of short (<10 peptide bonds) intrachain loops around the heme group.
Publication Date: 2002-01-23 PubMed ID: 11802740DOI: 10.1021/bi011371aGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- Non-P.H.S.
Summary
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This research examines how the histidine components of a specific protein, cytochrome c, bind to heme (an iron-containing component of hemoglobin) within microseconds when unfolded. These histidine components contribute significantly to the rapid kinetic changes observed in previous studies on cytochrome c’s dynamics.
Research Objectives and Methodology
- The research used spectroscopic studies to observe the behavior of histidine-26 and histidine-33 in unfolded horse iron(II) cytochrome c. These components were found to bind rapidly to the heme iron after a carbon monoxide (CO) ligand was detached.
- Researchers used four variants of cytochrome c (horse wild type, horse H33N, horse H33N/H26Q, and tuna wild type), which had been unfolded in the presence of guanidine hydrochloride at a pH of 6.5.
- Through these models, the team sought to demonstrate the effect of the histidine side chains on the observed microsecond spectral changes.
Key Findings
- As His33 and His26 were removed from the wild type sequence, the absorption spectra showed a systematic suppression of a rapid Soret absorbance change (associated with a rapid CO photolysis).
- It was concluded that this transient binding of histidine side chains to the heme causes one of the fast kinetic phases observed in previous photochemically triggered spectroscopic studies of iron(II) cytochrome c dynamics.
- Both His33 and His26 were found to equally impact the early kinetics.
Conclusion
- The study found that the stiffness of the polypeptide chain generated a deviation from Gaussian chain behaviour, slowing but not completely preventing, the formation of short intrachain loops around the heme group.
- This contributes to understanding how the specific structure and properties of a protein can impact how it interacts with other biological substances, and it also provides a clear demonstration of the rapid binding activity of these histidine sidechains in the context of cytochrome c function.
Cite This Article
APA
Hagen SJ, Latypov RF, Dolgikh DA, Roder H.
(2002).
Rapid intrachain binding of histidine-26 and histidine-33 to heme in unfolded ferrocytochrome C.
Biochemistry, 41(4), 1372-1380.
https://doi.org/10.1021/bi011371a Publication
Researcher Affiliations
- Physics Department, University of Florida, P.O. Box 118440, Gainesville, Florida 32611, USA. sjhagen@ufl.edu
MeSH Terms
- Animals
- Cytochrome c Group / chemistry
- Cytochrome c Group / metabolism
- Fishes
- Heme / metabolism
- Histidine / metabolism
- Horses
- Kinetics
- Protein Binding
- Protein Denaturation
- Spectrum Analysis
Citations
This article has been cited 12 times.- Hsu DJ, Leshchev D, Rimmerman D, Hong J, Kelley MS, Kosheleva I, Zhang X, Chen LX. X-ray snapshots reveal conformational influence on active site ligation during metalloprotein folding.. Chem Sci 2019 Nov 14;10(42):9788-9800.
- Mendez DL, Babbitt SE, King JD, D'Alessandro J, Watson MB, Blankenship RE, Mirica LM, Kranz RG. Engineered holocytochrome c synthases that biosynthesize new cytochromes c.. Proc Natl Acad Sci U S A 2017 Feb 28;114(9):2235-2240.
- Lee ES, Fung S, Sze-To HY, Wong AK. Discovering co-occurring patterns and their biological significance in protein families.. BMC Bioinformatics 2014;15 Suppl 12(Suppl 12):S2.
- Kim TW, Kim JG, Yang C, Ki H, Jo J, Ihee H. Pump-Probe X-ray Solution Scattering Reveals Accelerated Folding of Cytochrome c Upon Suppression of Misligation.. Bull Korean Chem Soc 2014 Mar 1;35(3):695-696.
- Harvilla PB, Wolcott HN, Magyar JS. The structure of ferricytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H.. Metallomics 2014 Jun;6(6):1126-30.
- Zaidi S, Hassan MI, Islam A, Ahmad F. The role of key residues in structure, function, and stability of cytochrome-c.. Cell Mol Life Sci 2014 Jan;71(2):229-55.
- Latypov RF, Maki K, Cheng H, Luck SD, Roder H. Folding mechanism of reduced Cytochrome c: equilibrium and kinetic properties in the presence of carbon monoxide.. J Mol Biol 2008 Nov 7;383(2):437-53.
- Kim S, Chung JK, Kwak K, Bowman SE, Bren KL, Bagchi B, Fayer MD. Native and unfolded cytochrome c--comparison of dynamics using 2D-IR vibrational echo spectroscopy.. J Phys Chem B 2008 Aug 14;112(32):10054-63.
- Chertkova RV, Sharonov GV, Feofanov AV, Bocharova OV, Latypov RF, Chernyak BV, Arseniev AS, Dolgikh DA, Kirpichnikov MP. Proapoptotic activity of cytochrome c in living cells: effect of K72 substitutions and species differences.. Mol Cell Biochem 2008 Jul;314(1-2):85-93.
- Abel CJ, Goldbeck RA, Latypov RF, Roder H, Kliger DS. Conformational equilibration time of unfolded protein chains and the folding speed limit.. Biochemistry 2007 Apr 3;46(13):4090-9.
- Jaspe J, Hagen SJ. Do protein molecules unfold in a simple shear flow?. Biophys J 2006 Nov 1;91(9):3415-24.
- Droghetti E, Oellerich S, Hildebrandt P, Smulevich G. Heme coordination states of unfolded ferrous cytochrome C.. Biophys J 2006 Oct 15;91(8):3022-31.
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