(Q47857138)

English

Functional role of heme ligation in cytochrome c. Effects of replacement of methionine 80 with natural and non-natural residues by semisynthesis

scientific article published on February 25, 1992

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/1310985

Functional role of heme ligation in cytochrome c. Effects of replacement of methionine 80 with natural and non-natural residues by semisynthesis (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1310985

11 September 2022

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10.1016/S0021-9258(19)50604-4

https://api.crossref.org/works/10.1016/S0021-9258(19)50604-4

1 December 2023

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10.1016/S0021-9258(19)50604-4

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1 December 2023

author name string

C. J. Wallace

1

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1310985

11 September 2022

I. Clark-Lewis

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1310985

11 September 2022

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1 February 1992

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6 February 2018

http://europepmc.org/abstract/MED/1310985

25 February 1992

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1310985

11 September 2022

full work available at URL

http://intl.jbc.org/cgi/content/abstract/267/6/3852

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1310985

11 September 2022

https://doi.org/10.1016/s0021-9258(19)50604-4

online access status

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1310985

1 December 2023

https://api.elsevier.com/content/article/PII:S0021925819506044?httpAccept=text/xml

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10.1016/S0021-9258(19)50604-4

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1 December 2023

https://api.elsevier.com/content/article/PII:S0021925819506044?httpAccept=text/plain

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10.1016/S0021-9258(19)50604-4

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1 December 2023

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/1310985

267

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/1310985

6

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Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/1310985

3852-3861

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/1310985

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

1

1 reference

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Automated chemical synthesis of a protein growth factor for hemopoietic cells, interleukin-3.

3

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Cleavage of cytochrome c with cyanogen bromide

4

1 reference

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Reconstitution of horse heart cytochrome c: interaction of the components obtained upon cleavage of the peptide bond following methionine residue 65

5

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The specificity and Kd at physiological ionic strength of an ATP-binding site on cytochrome c suit it to a regulatory role

6

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Role of arginine-38 in regulation of the cytochrome c oxidation-reduction equilibrium

7

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Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c

9

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A theoretical model for the effects of local nonpolar heme environments on the redox potentials in cytochromes

11

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Chemical synthesis of peptides and proteins

12

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High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c

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Role of phenylalanine-82 in yeast iso-1-cytochrome c and remote conformational changes induced by a serine residue at this position

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Control of redox properties of cytochrome c by special electrostatic interactions

16

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Structural basis for the variation in redox potential of cytochromes

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Semisynthesis of cytochrome c analogues. The effect of modifying the conserved residues 38 and 39.

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Axial ligand replacement in horse heart cytochrome c by semisynthesis.

24

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Experimental evaluation of the effective dielectric constant of proteins

26

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Structure and Function of Cytochromes C

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Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction.

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Haem exposure as the determinate of oxidation-reduction potential of haem proteins

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Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution

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Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 A and comparison with the ferrocytochrome structure

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Semisynthesis of horse heart cytochrome c analogues from two or three fragments

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Alkylamine derivatives of cytochrome c. Comparison with other lysine-modified analogues illuminates structure/function relations in the protein

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On the relationship between oxidation-reduction potential and biological activity in cytochrome c analogues. Results from four novel two-fragment complexes

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 February 2018

http://europepmc.org/abstract/MED/1310985

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