High-resolution three-dimensional structure of horse heart cytochrome c

Bushnell, Gordon W.; Louie, G.V.; Brayer, G.D.

doi:10.1016/0022-2836(90)90200-6

Cited by 1,027 publications

(1,029 citation statements)

References 41 publications

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“…This unfolding is substantial for the charge states reported here since the calculated cross section of the x-ray structure [17] and the solution NMR structure [18] is about 1350 Å 2 [12]. However, the results of Shelimov et al indicate the lowest charge states they investigated (3ϩ to 5ϩ) are substantially more compact than the native structure with cross sections of ϳ1200 Å 2 .…”

Section: Myoglobin and Cytochrome Cmentioning

confidence: 52%

Conformations of biopolymers in the gas phase: a new mass spectrometric method

Gill

Jennings

Wyttenbach

et al. 2000

International Journal of Mass Spectrometry

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A method is developed for measuring collision cross sections of gas-phase biomolecules using a slightly modified commercial triple quadrupele instrument. The modifications allow accurate stopping potentials to be measured for ions exiting the collision region of the instrument. A simple model allows these curves to be converted to cross sections. In order to account for certain poorly defined experimental parameters (exact ion energy, absolute pressure in the collision cell, etc.) variable parameters are included in the model. These parameters are determined on a case by case basis by normalizing the results to the well known cross section of singly charged bradykinin. Two relatively large systems were studied (cytochrome c and myoglobin) so comparisons could be made to literature values. A number of new peptide systems were then studied in the 9 -14 residue range. These included singly and doubly charged ions of luteinizing hormone releasing hormone (LHRH) substance P, and bombesin in addition to bradykinin. The experimental cross sections were in very good agreement with predictions from extensive molecular dynamics modeling. One interesting result was the experimental observation that the cross section of the doubly charged ions of LHRH, substance P, and bombesin were all smaller than those of the corresponding singly charged ions. Molecular dynamics did not reproduce this result, predicting doubly charged cross sections of the same magnitude or slightly larger than for the singly charged species. The experimental results appear to be correct, however. Possible shortcomings in the modeling procedure for multiply charged ions were suggested that might account for the discrepancy. (Int J Mass Spectrom 195/196 (2000) 685-697)

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Section: Myoglobin and Cytochrome Cmentioning

confidence: 52%

Conformations of biopolymers in the gas phase: a new mass spectrometric method

Gill

Jennings

Wyttenbach

et al. 2000

International Journal of Mass Spectrometry

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“…The results summarized above show that the folding reactions of iso-2 and horse cytochrome c respond very differently to changes that affect heme ligation, despite the fact that both have unfolded states with non-native histidine-heme ligands and three-dimensional structures with almost identical backbone folding (Bushnell et al, 1990;Murphy et al, 1992). There are two alternate explanations for the differences in folding: (1) the hypothesis that non-native histidine-heme ligation interferes with fast folding is incorrect, or (2) mechanistic differences in folding result in different effects of non-native heme ligation for iso-2 and horse cytochrome c. To test whether incorrect heme ligation slows down folding of yeast iso-2 cytochrome c, we have constructed a mutant protein (H33N,H39K iso-2) in which both potential non-native histidine-heme ligands are replaced.…”

Section: ~-_ _ _ _mentioning

confidence: 99%

Fast folding of cytochromec

Pierce

Nall

1997

Protein Science

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Native iso-2 cytochrome c contains two residues (His 18, Met 80) coordinated to the covalently attached heme. On unfolding of iso-2, the His I8 ligand remains coordinated to the heme iron, whereas Met 80 is displaced by a non-native heme ligand, His 33 or His 39. To test whether non-native His-heme ligation slows folding, we have constructed a double mutant protein in which the non-native ligands are replaced by asparagine and lysine, respectively (H33N,H39K iso-2). The double mutant protein, which cannot form non-native histidine-heme coordinate bonds, folds significantly faster than normal iso-2 cytochrome c: T = 14-26 ms for H33N,H39K iso-2 versus T = 200-1,100 ms for iso-2. These results with iso-2 cytochrome c strongly support the hypothesis that non-native His-heme ligation results in a kinetic barrier to fast folding of cytochrome c. Assuming that the maximum rate of a conformational search is about 10" s", the results imply that the direct folding pathway of iso-2 involves passage through on the order of lo9 or fewer partially folded conformers.

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“…Moreover, high-resolution crystal structures or NMR structural data are available, making them ideal candidates for such an investigation. [36][37][38][39][40] Albumin, known to transport numerous important biomolecules and drugs in the cytoplasm, 41 and transferrin, which controls the level of free iron in biological fluids, may react immediately with the metallaprisms, if they are administrated intravenously. Cytosolic proteins also possess important functions: cytochrome c is involved in apoptotic pathways, 42 while ubiquitin is relevant in posttranslational modifications together with the proteasome system, 43 and myoglobin is the primary oxygen-carrying pigment of muscle tissues.…”

Section: Introductionmentioning

confidence: 99%

Interactions of arene ruthenium metallaprisms with human proteins

2015

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Interactions between three hexacationic arene ruthenium metallaprisms, [( p-cymene) 6+ , and a series of human proteins including human serum albumin, transferrin, cytochrome c, myoglobin and ubiquitin have been studied using NMR spectroscopy, mass spectrometry and circular dichroism spectroscopy. All data suggest that no covalent adducts are formed between the proteins and the metallaprisms. Indeed, in most cases electrostatic interactions, leading to precipitation of protein-metallaprism aggregates, have been observed. In addition, with the smallest proteins, ubiquitin, myoglobin and cytochrome c, the presence of the hexacationic arene ruthenium metallaprisms induces structural changes of the proteins, as emphasized by circular dichroism. The results suggest that proteins are certainly a biological target for these metalla-assemblies.

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High-resolution three-dimensional structure of horse heart cytochrome c

Cited by 1,027 publications

References 41 publications

Conformations of biopolymers in the gas phase: a new mass spectrometric method

Conformations of biopolymers in the gas phase: a new mass spectrometric method

Fast folding of cytochromec

Interactions of arene ruthenium metallaprisms with human proteins

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