c-Type Cytochrome Biogenesis Can Occur via a Natural Ccm System Lacking CcmH, CcmG, and the Heme-binding Histidine of CcmE

Goddard, Alan D.; Stevens, Julie M.; Rao, Feng; Mavridou, Despoina A. I.; Chan, Wee Lee; Richardson, David J.; Allen, James W. A.; Ferguson, Stuart J.

doi:10.1074/jbc.m110.133421

Cited by 24 publications

(33 citation statements)

References 49 publications

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“…We conclude that under the aerobic conditions used, both recombinant systems II and III require some thiol reduction and this periplasmic reduction is mediated by the natural E.coli DsbC and/or DsbD proteins. For system III, the lack of a strong DsbD requirement suggests that DsbC may be acting in a DsbD-independent manner, thus DsbC can obtain reductant from other periplasmic proteins directly or from reduced DsbA, as shown previously [63, 64]. In addition to the thiol reduction requirement, DsbC might protect the apocytochrome c cysteines from sulfenylation, which was recently reported as a function of DsbC [65].…”

Section: Resultsmentioning

confidence: 66%

Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III

Richard-Fogal

Francisco

Frawley

et al. 2012

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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The reconstitution of biosynthetic pathways from heterologous hosts can help define the minimal genetic requirements for pathway function and facilitate detailed mechanistic studies. Each of the three pathways for the assembly of cytochrome c in nature (called systems I, II, and III) has been shown to function recombinantly in Escherichia coli, covalently attaching heme to the cysteine residues of a CXXCH motif of a c-type cytochrome. However, recombinant systems I (CcmABCDEFGH) and II (CcsBA) function in the E. coli periplasm, while recombinant system III (CCHL) attaches heme to its cognate receptor in the cytoplasm of E. coli, which makes direct comparisons between the three systems difficult. Here we show that the human CCHL (with a secretion signal) attaches heme to the human cytochrome c (with a signal sequence) in the E.coli periplasm, which is bioenergetically (p-side) analogous to the mitochondrial intermembrane space. The human CCHL is specific for the human cytochrome c, whereas recombinant system II can attach heme to multiple non-cognate c-type cytochromes (possessing the CXXCH motif.) We also show that the recombinant periplasmic systems II and III use components of the natural E.coli periplasmic DsbC/DsbD thiol-reduction pathway.

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Section: Resultsmentioning

confidence: 66%

Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III

Richard-Fogal

Francisco

Frawley

et al. 2012

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…Finally, why the species with a His to Cys variant of CcmE also lack CcmG and CcmH ( see below ) [77], how the reduced heme-iron (Fe 2+ ) is conveyed to CcmC subsequent to its synthesis by ferrochelatase, and whether ATP hydrolysis by CcmAB is required to transport an unknown compound, remain elusive.…”

Section: Ccm-system I: Functional Organizationmentioning

confidence: 99%

Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

Verissimo

Daldal

2014

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Cytochromes c are ubiquitous heme proteins that are found in most living organisms and are essential for various energy production pathways as well as other cellular processes. Their biosynthesis relies on a complex post-translational process, called cytochrome c biogenesis, responsible for the formation of stereo-specific thioether bonds between the vinyl groups of heme b (protoporphyrin IX-Fe) and the thiol groups of apocytochromes c heme-binding site (C1XXC2H) cysteine residues. In some organisms this process involves up to nine (CcmABCDEFGHI) membrane proteins working together to achieve heme ligation, designated the Cytochrome c maturation (Ccm)-System I. Here, we review recent findings related to the Ccm-System I found in bacteria, archaea and plant mitochondria, with an emphasis on protein interactions between the Ccm components and their substrates (apocytochrome c and heme). We discuss the possibility that the Ccm proteins may form a multi subunit supercomplex (dubbed “Ccm machine”), and based on the currently available data, we present an updated version of a mechanistic model for Ccm.

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“…The most familiar example is provided by c -type cytochromes, which are biosynthesized from apocytochrome and b heme and contain one or two thioether bonds to cysteines. Interestingly, the maturation of cytochrome c via system I (CcmABCDEFGH) proceeds with transient heme attachment to a histidine or a cysteine of CcmE [15]. The nature of the CcmE histidine adduct has been elucidated: the reversible linkage is between the N δ 1 atom and the heme 2-C β [16], unlike in GlbN-A.…”

Section: Introductionmentioning

confidence: 99%

Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination

et al. 2011

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In the absence of an exogenous ligand, the hemoglobins from the cyanobacteria Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 coordinate the heme group with two axial histidines (His46 and His70). These globins also form a covalent linkage between the heme 2-vinyl substituent and His117. The in vitro mechanism of heme attachment to His117 was examined with a combination of site-directed mutagenesis, NMR spectroscopy, and optical spectroscopy. The results supported an electrophilic addition with vinyl protonation being the rate-determining step. Replacement of His117 with a cysteine demonstrated that the reaction could occur with an alternative nucleophile. His46 (distal histidine) was implicated in the specificity of the reaction for the 2-vinyl group as well as protection of the protein from oxidative damage caused by exposure to exogenous H2O2.

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c-Type Cytochrome Biogenesis Can Occur via a Natural Ccm System Lacking CcmH, CcmG, and the Heme-binding Histidine of CcmE

Cited by 24 publications

References 49 publications

Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III

Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III

Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination

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