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Maturation of Plastid c-type Cytochromes
by
Gabilly, Stéphane T.
, Hamel, Patrice P.
in
Algae
/ Bacteria
/ BASIC BIOLOGICAL SCIENCES
/ Binding
/ Binding sites
/ Catalysis
/ Cyanobacteria
/ Cytochrome
/ cytochrome b6f
/ Cytochrome c
/ Cytochromes
/ Deficient mutant
/ Genetic analysis
/ Heme
/ hylakoid lumen
/ Ligands
/ Membrane proteins
/ Membranes
/ Photosynthesis
/ Plant Science
/ Plastids
/ Prostheses
/ Proteins
/ Stroma
/ thioether
/ thylakoid lumen
/ Thylakoid membranes
2017
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Maturation of Plastid c-type Cytochromes
by
Gabilly, Stéphane T.
, Hamel, Patrice P.
in
Algae
/ Bacteria
/ BASIC BIOLOGICAL SCIENCES
/ Binding
/ Binding sites
/ Catalysis
/ Cyanobacteria
/ Cytochrome
/ cytochrome b6f
/ Cytochrome c
/ Cytochromes
/ Deficient mutant
/ Genetic analysis
/ Heme
/ hylakoid lumen
/ Ligands
/ Membrane proteins
/ Membranes
/ Photosynthesis
/ Plant Science
/ Plastids
/ Prostheses
/ Proteins
/ Stroma
/ thioether
/ thylakoid lumen
/ Thylakoid membranes
2017
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Maturation of Plastid c-type Cytochromes
by
Gabilly, Stéphane T.
, Hamel, Patrice P.
in
Algae
/ Bacteria
/ BASIC BIOLOGICAL SCIENCES
/ Binding
/ Binding sites
/ Catalysis
/ Cyanobacteria
/ Cytochrome
/ cytochrome b6f
/ Cytochrome c
/ Cytochromes
/ Deficient mutant
/ Genetic analysis
/ Heme
/ hylakoid lumen
/ Ligands
/ Membrane proteins
/ Membranes
/ Photosynthesis
/ Plant Science
/ Plastids
/ Prostheses
/ Proteins
/ Stroma
/ thioether
/ thylakoid lumen
/ Thylakoid membranes
2017
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Journal Article
Maturation of Plastid c-type Cytochromes
2017
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Overview
Cytochromes
are hemoproteins, with the prosthetic group covalently linked to the apoprotein, which function as electron carriers. A class of cytochromes
is defined by a C
CH heme-binding motif where the cysteines form thioether bonds with the vinyl groups of heme. Plastids are known to contain up to three cytochromes
. The membrane-bound cytochrome
and soluble cytochrome
operate in photosynthesis while the activity of soluble cytochrome
remains unknown. Conversion of apo- to holocytochrome
occurs in the thylakoid lumen and requires the independent transport of apocytochrome and heme across the thylakoid membrane followed by the stereospecific attachment of ferroheme via thioether linkages. Attachment of heme to apoforms of plastid cytochromes
is dependent upon the products of the
(for
ytochrome
ynthesis) genes, first uncovered via genetic analysis of photosynthetic deficient mutants in the green alga
. The CCS pathway also occurs in cyanobacteria and several bacteria. CcsA and CCS1, the signature components of the CCS pathway are polytopic membrane proteins proposed to operate in the delivery of heme from the stroma to the lumen, and also in the catalysis of the heme ligation reaction. CCDA, CCS4, and CCS5 are components of trans-thylakoid pathways that deliver reducing equivalents in order to maintain the heme-binding cysteines in a reduced form prior to thioether bond formation. While only four CCS components are needed in bacteria, at least eight components are required for plastid cytochrome
assembly, suggesting the biochemistry of thioether formation is more nuanced in the plastid system.
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