Increase in apparent compressibility of cytochrome c upon oxidation.

Eden, Don; Matthew, James B.; Rosa, Joseph J.; Richards, Frederic M.

doi:10.1073/pnas.79.3.815

Cited by 94 publications

(62 citation statements)

References 38 publications

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“…[184][185][186] Ultrasonic velocimetry was used to measure the root mean square volume fluctuations and apparent molal and adiabatic compressibilities of ferro-and ferricytochrome c. 185 The compressibilities and volume fluctuations were greater for the oxidized form indicating increased flexibility. Recently, however, Sagle et al 187 elegantly demonstrated using site directed isotope labeling and FTIR that oxidation of Cyt C residues near the heme moiety increases local protein unfolding without increasing flexibility.…”

Section: Oxidationmentioning

confidence: 99%

The Complex Inter-Relationships Between Protein Flexibility and Stability

Kamerzell¹,

Middaugh²

2008

Journal of Pharmaceutical Sciences

105

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Section: Oxidationmentioning

confidence: 99%

The Complex Inter-Relationships Between Protein Flexibility and Stability

Kamerzell¹,

Middaugh²

2008

Journal of Pharmaceutical Sciences

105

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“…4 graphic evidence shows that there are small differences between the tertiary structures of MetMb and deoxy Mb (15,16); moreover, in the former, H20 is the sixth ligand, whereas, in the latter, the iron has only five ligands. Recent measurements of compressibility in cytochrome c point to a substantial difference in dynamic properties between the ferri and ferro forms of the protein, despite the identical time-averaged structure of these proteins (25). Therefore, it is, perhaps not surprising to find differences in dynamics between MetMb and deoxy Mb.…”

mentioning

confidence: 91%

Dynamics of heme iron in crystals of metmyoglobin and deoxymyoglobin.

Bauminger¹,

Cohen²,

Nowik³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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The 57Fe v-ray resonance absorption spectra have been measured in crystals of metmyoglobin and deoxymyoglobin over a wide range of temperatures. Above a critical temperature common to both proteins (220 K), the dynamics of heme iron display a dramatic change, in that two kinds of thermal fluctuations come into play-a fast fluctuation associated with a steep decrease of the total resonance absorption with increasing temperature, and a slower fluctuation of characteristic time 10-8 sec, associated with bounded diffusive motion. By using both discrete jump and continuous diffusion models, the latter based on the Brownian motion of an overdamped harmonic oscillator, the essential parameters of the iron motion (mean square displacement andjump frequency or diffusion constant) can be derived as a function oftemperature. Thus, for deoxy Mb at 288 K, the mean square displacement for the fast fluctuation is about 6 x 10-2 A and for the diffusive motion is 1.6 x 10-2 A2; the diffusion constant is 4 X 10-10 cm2/sec. The diffusive process is associated with an activation energy ofabout 0.75 kcal/mol. Although the same general kinds of phenomena are observed in crystals of MetMb and deoxy Mb, significant differences in behavior are found, which suggest that the main dynamical phenomenon observed reflects internal large-scale motions of the protein.There has been a rapidly growing interest in recent years in the study of the dynamics of structural fluctuations and conformational changes in proteins (1). These studies, which extend our knowledge beyond the time-averaged models of protein structure obtained by x-ray diffraction from protein crystals, are important in understanding aspects of the biological function of proteins. A variety of techniques, appropriate to different time scales, have been used in experimental investigations of the dynamics of proteins (1). The analysis of the x-ray diffraction temperature factors from crystals of some globular proteins (2, 3) has provided valuable information concerning the mean square displacement (msd), (x2), of atoms in different parts of the protein.The dynamics of active sites in proteins are of particular interest. In this respect, Mossbauer resonance absorption spectroscopy has been especially useful in the study ofthe dynamics of iron atoms in iron proteins. From the recoilless fraction f, estimates of the msd of the iron atoms can be obtained. Information on the dependence of (x2) on temperature has been obtained in this way for oxy Mb in frozen solution (4) and for crystals of MetMb (5, 6) and deoxy Mb (7). Rayleigh-Mossbauer scattering also has been used to investigate the dynamics of Mb (8,9). Recent investigations of the 57Fe y-ray absorption spectrum over an extended range of scanning velocities in crystals of the proteins ferritin (10-12), MetMb (11,12), and HbCO (13) have revealed striking new phenomena highly pertinent to the dynamics of iron in these proteins.In this paper we present the results ofa detailed investigation and comparison of these phenomena i...

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“…For cytochrome c the differences in the effective radii of the oxidized and reduced states are thought to result from a combination of electrostatic and conformational changes. Small structural differences have been identified between the two redox forms of cytochrome c (25,26). In addition it has been suggested that phosphate binding to lysine-rich sites at low ionic strengths in the oxidized state may contribute to the increase in the effec- 1 The abbreviation used is: ANS, 8-anilino-1-napthalenesulphonate.…”

Section: Thementioning

confidence: 99%

The Cytochrome c Fold Can Be Attained from a Compact Apo State by Occupancy of a Nascent Heme Binding Site

Wain¹,

Pertinhez²,

Tomlinson³

et al. 2001

Journal of Biological Chemistry

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NMR techniques and 8-anilino-1-napthalenesulphonate (ANS) binding studies have been used to characterize the apo state of a variant of cytochrome c 552 from Hydrogenobacter thermophilus. In this variant the two cysteines that form covalent thioether linkages to the heme group have been replaced by alanine residues (C11A/C14A). CD studies show that the apo state contains ϳ14% helical secondary structure, and measurements of hydrodynamic radii using pulse field gradient NMR methods show that it is compact (R h , 16.6 Å). The apo state binds 1 mol of ANS/mol of protein, and a linear reduction in fluorescence enhancement is observed on adding aliquots of hemin to a solution of apo C11A/C14A cytochrome c 552 with ANS bound. These results suggest that the bound ANS is located in the heme binding pocket, which would therefore be at least partially formed in the apo state. Consistent with these characteristics, the formation of the holo state of the variant cytochrome c 552 from the apo state on the addition of heme has been demonstrated using NMR techniques.

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Increase in apparent compressibility of cytochrome c upon oxidation.

Abstract: BiophysicsIncrease in apparent compressibility of cytochrome c upon oxidation (

Cited by 94 publications

References 38 publications

The Complex Inter-Relationships Between Protein Flexibility and Stability

The Complex Inter-Relationships Between Protein Flexibility and Stability

Dynamics of heme iron in crystals of metmyoglobin and deoxymyoglobin.

The Cytochrome c Fold Can Be Attained from a Compact Apo State by Occupancy of a Nascent Heme Binding Site

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