Ferricytochrome c

Dickerson, Richard E.; Takano, Tsunehiro; Eisenberg, David; Kallai, Olga B.; Samson, Linus Manu; Cooper, Angela; Margoliash, E.

doi:10.1016/s0021-9258(19)77002-1

Cited by 881 publications

(177 citation statements)

References 65 publications

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“…Â precipitate, formed over several hours, was washed with cold water. The ISp NMR spectrum of the solid dissolved in DMF showed it to consist of more than 95% of the cis isomer and of a very small amount of the trans isomer, exactly as reported originally (38). The subsequent treatment of [Pt(2-Fpy)4]2+with HQ yielded not the pure ^^/Z!r-[Pt(2-Fpy)2C!l2l as was Âe case with the pyridine ligand, but a mixture of cisand £rdwy-[Pt(2-Fpy)2Cl2].…”

Section: B Cytochrome Fsupporting

confidence: 84%

“…Horse heart cytochrome fis a 12.5 kDa, single-chain, iron heme protein (38,39); it is well characterized and commercially available. Its physiological role, in the eukaryotic mitochondrial respiratory chain, is as a one-electron shuttle between the membrane-bound complexes cytochrome c reductase and cytochrome c oxidase; the latter is the terminal component which reduces molecular oxygen to water.…”

Section: B Cytochrome Fmentioning

confidence: 99%

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Cross-linked metalloproteins: Novel systems for the study of intraprotein electron-transfer reactions

Peerey¹

1990

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The most advanced technology has been used to photo graph and reproduce this manuscript from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. F. Intracomplex Electron-Transfer Reactions 1. Overview of the reactions 2. Electrostatic complex: pulse radiolysis experiments 3. Electrostatic complex; flash photolysis experiments 4. Covalent complex: pulse radiolysis experiments 5. Covalentcomplex: flash photolysis experiments G. Reactivity of the Covalent cyt^c Complexes n. Conclusions V. NOVEL COMPLEXES OF CYTOCHROME C

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Section: B Cytochrome Fsupporting

confidence: 84%

Section: B Cytochrome Fmentioning

confidence: 99%

Cross-linked metalloproteins: Novel systems for the study of intraprotein electron-transfer reactions

Peerey¹

1990

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“…Pc, a 104-amino acid protein, contains 18 lysine residues (Fig. 1) spaced relatively evenly across the length of the polypeptide chain (40). Thus, after methylation to introduce 3H, most peptide fragments of Pc resulting from processing will be radiolabded and therefore can be detected.…”

Section: Resultsmentioning

confidence: 99%

Biochemical evidence for the rapid assembly and disassembly of processed antigen-major histocompatibility complex class II complexes in acidic vesicles of B cells.

Marsh

Dalke

Pierce

1992

The Journal of Experimental Medicine

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SummaryHelper T cell recognition of antigen requires that it be processed within antigen-presenting cells (APC) to peptide fragments that subsequently bind to major histocompatibility complex (MHC) class II molecules and are displayed on the APC surface. Heretofore, processed antigen-MHC class II complexes have been detected by functional assays, measuring the activation of specific T cells. We now report direct, biochemical evidence for the assembly of processed antigen-MHC class II complexes within splenic B ceils as APC. The I-E k MHC class II molecules were immunoprecipitated from B cells that had processed the model protein antigen cytochrome c radiolabeled across its entire length by reductive methylation of lysine residues and covalently coupled to Ig-specific antibodies, allowing internalization after binding to surface Ig. Our previous studies showed that I-E ~ immunoaffinity purified from B cells that had processed cytochrome c contains functional processed antigen-MHC class II complexes and that approximately 0.2% of the I-E k molecules are specifically associated with one of two predominant processed antigenic fragments. Here we show that these complexes are rapidly assembled, within 30--60 min after antigen binding to surface Ig on splenic B cells. Maximal numbers of complexes are assembled by 2 h in a process that is sensitive to acidic vesicle inhibitors but not to inhibitors of protein synthesis. The processed antigen-I-E k complexes have a relatively short half-life of 2--4 h and are disassembled or degraded within 8 h after antigen is first internalized. The disassembly or degradation of the processed antigen-I-E k complexes requires acidic vesicle function, and in the presence of an acidic vesicle inhibitor the complexes are long lived. Thus, using a biochemical assay to monitor processed antigen-I-E k complexes, we find that, in B cells, processed antigen is relatively rapidly associated in acidic vesicles with preexisting MHC class II molecules, and the complexes are disassembled 4-6 h later in processes that also require acid vesicle function.

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“…Met and His are coordinated to the haem iron in the cyt c monomer. 58,59 In contrast, haem-coordinating Met80 disassociates from the haem iron in the cyt c 3D-DS dimer and trimer; thus, external ligands, such as the cyanide ion, bind more easily to the haem iron of oligomers than to that of the monomer. 60 Peroxides may also bind to the haem iron of cyt c oligomer more easily, making the peroxidase activity of the cyt c dimer higher than that of the monomer, 61 which is consistent with the fact that the peroxidase activity of cyt c increases when Met80 dissociates from the haem iron, which may be relevant to apoptosis.…”

Section: D Domain Swapping Of Native Metalloproteinsmentioning

confidence: 99%