The interaction between heme and protein in cytochrome c1

Tervoort, M.J.; Gelder, B.F. Van

doi:10.1016/0005-2728(83)90166-4

Cited by 5 publications

(1 citation statement)

References 31 publications

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“…Cysteine is important in some patterns of zinc and copper coordination, in stabilizing iron-sulfur clusters and in covalent attachments to heme in many cytochrome structures (8). Cysteine also contributes in mediating protein-DNA interactions such as occur with zinc fingers and ring fingers (9, 10).…”

Section: Resultsmentioning

confidence: 99%

Atom density in protein structures

Karlin

Zhu

Baud

1999

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

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The residue environment in protein structures is studied with respect to the density of carbon (C), oxygen (O), and nitrogen (N) atoms within a certain distance (say 5 Å) of each residue. Two types of environments are evaluated: one based on side-chain atom contacts (abbreviated S-S) and the other based on all atom (sidechain ؉ backbone) contacts (abbreviated A-A). Different atom counts are observed about nine-residue structural categories defined by three solvent accessibility levels and three secondary structure states. Among the structural categories, the S-S atom count ratios generally vary more than the A-A atom count ratios because of the fact that the backbone (O) and (N) atoms contribute equal counts. Secondary structure affects the (C) density for the A-A contacts whereas secondary structure has little influence on the (C) density for the S-S contacts. For S-S contacts, a greater density of (O) over (N) atom neighbors stands out in the environment of most amino acid types. By contrast, for A-A contacts, independent of the solvent accessibility levels, the ratio (O)͞(N) is Ϸ1 in helical states, consistent with the geometry of ␣-helical residues whose side-chains tilt oppositely to the amino to carboxy ␣-helical axis. The highest ratio of neighbor (O)͞(N) is achieved under solvent exposed conditions. This (O) vs. (N) prevalence is advantageous at the protein surface that generally exhibits an acid excess that helps to enhance protein solubility in the cell and to avoid nonspecific interactions with phosphate groups of DNA, RNA, and other plasma constituents.residue associations ͉ oxygen ͉ nitrogen

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Section: Resultsmentioning

confidence: 99%

Atom density in protein structures

Karlin

Zhu

Baud

1999

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

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Structural Studies of Euglena Cytochrome C 1

1990

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The pet genes of Rhodospirillum rubrum: cloning and sequencing of the genes for the cytochrome bc 1-complex

Majewski

Trebst

1990

Molec. Gen. Genet.

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A cytochrome bc1-complex of Rs. rubrum was isolated and the three subunits were purified to homogeneity. The N-terminal amino acid sequence of the purified subunits was determined by automatic Edman degradation. The pet genes of Rhodospirillum rubrum coding for the three subunits of the cytochrome bc1-complex were isolated from a genomic library of Rs. rubrum using oligonucleotides specific for conserved regions of the subunits from other organisms and a heterologous probe derived from the genes for the complex of Rb. capsulatus. The complete nucleotide sequence of a 5500 bp SalI/SphI fragment is described which includes the pet genes and three additional unidentified open reading frames. The N-terminal amino acid sequence of the isolated subunits was used for the identification of the three genes. The genes encoding the subunits are organized as follows: Rieske protein, cytochrome b, cytochrome c1. Comparison of the N-terminal protein sequences with the protein sequences deduced from the nucleotide sequence showed that only cytochrome c1 is processed during transport and assembly of the three subunits of the complex. Only the N-terminal methionine of the Rieske protein is cleaved off. The similarity of the deduced amino acid sequence of the three subunits to the corresponding subunits of other organisms is described and implications for structural features of the subunits are discussed.

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The interaction between heme and protein in cytochrome c1

Cited by 5 publications

References 31 publications

Atom density in protein structures

Atom density in protein structures

Structural Studies of Euglena Cytochrome C 1

The pet genes of Rhodospirillum rubrum: cloning and sequencing of the genes for the cytochrome bc 1-complex

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