Summary
Detailed understanding of the regulation of cytochrome synthesis is an area that remains substantially undefined. Evidence to date suggests that the synthesis of cytochromes involves complex coordination of heme biosynthesis with expression of cytochrome apoproteins. Heme biosynthesis in turn is coordinated with the import of iron, as the presence of a coordinated iron in the heme tetrapyrrole is a key feature that allows heme to undertake redox reactions, redox sensing, and to carry diatomic gases such as O2, CO or NO. Some cytochrome oxidases also contain copper centers that are involved in shuttling electrons to and from heme groups. Since excess of iron and/or copper is toxic to cells, the proper import of these metals is also a significant consideration for the synthesis of some respiratory cytochromes. This review will cover both transcriptional and post-transcriptional control mechanisms that affect the synthesis of heme, the expression of cytochrome apoproteins and homeostasis of iron and copper in photosynthetic organisms.
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Abbreviations
- ALA:
-
δ−aminolevulinic acid
- BChl:
-
Bacteriochlorophyll
- cbb 3-Cox:
-
cbb 3 cytochrome oxidase
- Chl:
-
Chlorophyll
- Cys:
-
Cysteine
- DMSO:
-
Dimethyl sulfoxide
- GluTR:
-
Glutamyl-tRNA reductase
- PAS:
-
Per-Arnt-Sim
- PBG:
-
Porphobilinogen
- PPIX:
-
Protoporphyrin IX
- PS:
-
Photosystem
- Rb. :
-
Rhodobacter
References
Anzaldi LL, Skaar EP (2010) Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens. Infect Immun 78:4977–4989
Azzouzi A, Steunou A-S, Durand A, Khalfaoui-Hassani B, Bourbon M-L, Astier C, Bollivar DW, Ouchane S (2013) Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu+-ATPase mutant copA− of Rubrivivax gelatinosus. Mol Microbiol 88:339–351
Banerjee R, Ragsdale SW (2003) The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes. Annu Rev Biochem 72:209–247
Bauer CE, Elsen S, Bird TH (1999) Mechanisms for redox control of gene expression. Annu Rev Microbiol 53:495–523
Beale SI (1978) δ-Aminolevulinic acid in plants: its biosynthesis, regulation, and role in plastid development. Annu Rev Plant Physiol 29:95–120
Beale SI, Castelfranco PA (1973) 14 C incorporation from exogenous compounds into -aminolevulinic acid by greening cucumber cotyledons. Biochem Biophys Res Commun 52:143–149
Biel SW, Biel AJ (1990) Isolation of a Rhodobacter capsulatus mutant that lacks c-type cytochromes and excretes porphyrins. J Bacteriol 172:1321–1326
Bird TH, Du S, Bauer CE (1999) Autophosphorylation, phosphotransfer, and DNA-binding properties of the RegB/RegA two-component regulatory system in Rhodobacter capsulatus. J Biol Chem 274:16343–16348
Burnham BF, Lascelles J (1963) Control of porphyrin biosynthesis through a negative-feedback mechanism. Studies with preparations of δ-aminolaevulate synthetase and δ-aminolaevulate dehydratase from Rhodopseudomonas spheroides. Biochem J 87:462–472
Cheng Z, Wu J, Setterdahl A, Reddie K, Carroll K, Hammad LA, Karty JA, Bauer CE (2012) Activity of the tetrapyrrole regulator CrtJ is controlled by oxidation of a redox active cysteine located in the DNA binding domain. Mol Microbiol 85:734–746
Chereskin BM, Castelfranco PA (1982) Effects of iron and oxygen on chlorophyll biosynthesis: II. Observations on the biosynthetic pathway in isolated etiochloroplasts. Plant Physiol 69:112–116
Chiancone E, Ceci P, Ilari A, Ribacchi F, Stefanini S (2004) Iron and proteins for iron storage and detoxification. Biometals 17:197–202
Cornelis P, Wei Q, Andrews SC, Vinckx T (2011) Iron homeostasis and management of oxidative stress response in bacteria. Metallomics 3:540–549
Dupont CL, Grass G, Rensing C (2011) Copper toxicity and the origin of bacterial resistance – new insights and applications. Metallomics 3:1109–1118
Ekici S, Pawlik G, Lohmeyer E, Koch H-G, Daldal F (2012a) Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus. Biochim Biophys Acta 1817:898–910
Ekici S, Yang H, Koch H-G, Daldal F (2012b) Novel transporter required for biogenesis of cbb3-type cytochrome c oxidase in Rhodobacter capsulatus. mBio 3:e00293-11
Ekici S, Jiang X, Koch H-G, Daldal F (2013) Missense mutations in cytochrome c maturation genes provide new insights into Rhodobacter capsulatus cbb3-type cytochrome c oxidase biogenesis. J Bacteriol 195:261–269
Ekici S, Turkarslan S, Pawlik G, Dancis A, Baliga NS, Koch HG, Daldal F (2014) Intracytoplasmic copper homeostasis controls cytochrome c oxidase production. mBio 5:e01055-13
Elsen S, Ponnampalam SN, Bauer CE (1998) CrtJ bound to distant binding sites interacts cooperatively to aerobically repress photopigment biosynthesis and light harvesting II gene expression in Rhodobacter capsulatus. J Biol Chem 273:30762–30769
Eraso JM, Kaplan S (1994) prrA, a putative response regulator involved in oxygen regulation of photosynthesis gene expression in Rhodobacter sphaeroides. J Bacteriol 176:32–43
Eraso JM, Kaplan S (2000) From redox flow to gene regulation: role of the PrrC protein of Rhodobacter sphaeroides 2.4.1. Biochemistry 39:2052–2062
Ferreira F, Straus NA (1994) Iron deprivation in cyanobacteria. J Appl Phycol 6:199–210
Frankenberg N, Moser J, Jahn D (2003) Bacterial heme biosynthesis and its biotechnological application. Appl Microbiol Biotechnol 63:115–127
Fraser JM, Tulk SE, Jeans JA, Campbell DA, Bibby TS, Cockshutt AM (2013) Photophysiological and photosynthetic complex changes during iron starvation in Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942. PLoS One 3:e59861
Gomelsky M, Kaplan S (1995) Genetic evidence that PpsR from Rhodobacter sphaeroides 2.4.1 functions as a repressor of puc and bchF expression. J Bacteriol 177:1634–1637
González A, Bes MT, Valladares A, Peleato ML, Fillat MF (2012) FurA is the master regulator of iron homeostasis and modulates the expression of tetrapyrrole biosynthesis genes in Anabaena sp. PCC 7120. Environ Microbiol 14:3175–3187
Graça-Souza AV, Maya-Monteiro C, Paiva-Silva GO, Braz GRC, Paes MC, Sorgine MHF, Oliveira MF, Oliveira PL (2006) Adaptations against heme toxicity in blood-feeding arthropods. Insect Biochem Mol Biol 36:322–335
Grammel H, Ghosh R (2008) Redox-state dynamics of ubiquinone-10 imply cooperative regulation of photosynthetic membrane expression in Rhodospirillum rubrum. J Bacteriol 190:4912–4921
Hassani BK, Astier C, Nitschke W, Ouchane S (2010a) CtpA, a copper-translocating P-type ATPase involved in the biogenesis of multiple copper-requiring enzymes. J Biol Chem 295:19330–19337
Hassani BK, Steunou A-S, Liotenberg S, Reiss-Husson F, Astier C, Ouchane S (2010b) Adaptation to oxygen: role of terminal oxidases in photosynthesis initiation in the purple photosynthetic bacterium, Rubrivivax gelatinosus. J Biol Chem 285:19891–19899
Huang D-D, Wang W-y (1986a) Genetic control of chlorophyll biosynthesis: regulation of delta-aminolevulinate synthesis in Chlamydomonas. Mol Gen Genet 205:217–220
Huang D-D, Wang W-y (1986b) Chlorophyll biosynthesis in Chlamydomonas starts with the formation of glutamyl-tRNA. J Biol Chem 261:13451–13455
Inoue K, Kouadio JL, Mosley CS, Bauer CE (1995) Isolation and in vitro phosphorylation of sensory transduction components controlling anaerobic induction of light harvesting and reaction center gene expression in Rhodobacter capsulatus. Biochemistry 34:391–396
Karls RK, Brooks J, Rossmeissl P, Luedke J, Donohue TJ (1998) Metabolic roles of a Rhodobacter sphaeroides member of the sigma32 family. J Bacteriol 180:10–19
Karls RK, Wolf JR, Donohue TJ (1999) Activation of the cycA P2 promoter for the Rhodobacter sphaeroides cytochrome c2 gene by the photosynthesis response regulator. Mol Microbiol 34:822–835
Kim Y-J, Ko I-J, Lee J-M, Kang H-Y, Kim YM, Kaplan S, Oh J-I (2007) Dominant role of the cbb3 oxidase in regulation of photosynthesis gene expression through the PrrBA system in Rhodobacter sphaeroides 2.4.1. J Bacteriol 189:5617–5625
Klamt S, Grammel H, Straube R, Ghosh R, Gilles ED (2008) Modeling the electron transport chain of purple non-sulfur bacteria. Mol Syst Biol 4:1–19
Koch HG, Hwang O, Daldal F (1998) Isolation and characterization of Rhodobacter capsulatus mutants affected in cytochrome cbb3 oxidase activity. J Bacteriol 180:969–978
Kumar S, Bandyopadhyay U (2005) Free heme toxicity and its detoxification systems in human. Toxicol Lett 157:175–188
Kumar AM, Schaub U, Söll D, Ujwal ML (1996) Glutamyl-transfer RNA: at the crossroad between chlorophyll and protein biosynthesis. Trends Plant Sci 1:371–376
Lascelles J (1956) The synthesis of porphyrins and bacteriochlorophyll in cell suspensions of Rhodopseudomonas spheroides. Biochem J 62:78–93
Lascelles J (1960) The synthesis of enzymes concerned in bacteriochlorophyll formation in growing cultures of Rhodopseudomonas spheroides. J Gen Microbiol 23:487–498
Lascelles J, Hatch TP (1969) Bacteriochlorophyll and heme synthesis in Rhodopseudomonas spheroides: possible role of heme in regulation of the branched biosynthetic pathway. J Bacteriol 98:712–720
Lee S, Ryu J-Y, Kim SY, Jeon J-H, Song JY, Cho H-T, Choi S-B, …, Park YI (2007) Transcriptional regulation of the respiratory genes in the cyanobacterium Synechocystis sp. PCC 6803 during the early response to glucose feeding. Plant Physiol 145:1018–1030
Lohmeyer E, Schröder S, Pawlik G, Trasnea P-I, Peters A, Daldal F, Koch H-G (2012) The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb3-type cytochrome oxidase in Rhodobacter capsulatus. Biochim Biophys Acta 1817:2005–2015
MacGregor BJ, Karls RK, Donohue TJ (1998) Transcription of the Rhodobacter sphaeroides cycA P1 promoter by alternate RNA polymerase holoenzymes. J Bacteriol 180:1–9
Macomber L, Imlay JA (2009) The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. Proc Natl Acad Sci U S A 106:8344–8349
Masuda S, Bauer CE (2002) AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides. Cell 110:613–623
Masuda S, Dong C, Swem D, Setterdahl AT, Knaff DB, Bauer CE (2002) Repression of photosynthesis gene expression by formation of a disulfide bond in CrtJ. Proc Natl Acad Sci U S A 99:7078–7083
Meinecke L, Alawady A, Schroda M, Willows R, Kobayashi MC, Niyogi KK, Grimm B, Beck CF (2010) Chlorophyll-deficient mutants of Chlamydomonas reinhardtii that accumulate magnesium protoporphyrin IX. Plant Mol Biol 72:643–658
Moskvin OV, Gomelsky L, Gomelsky M (2005) Transcriptome analysis of the Rhodobacter sphaeroides PpsR regulon: PpsR as a master regulator of photosystem development. J Bacteriol 187:2148–2215
Mosley CS, Suzuki JY, Bauer CE (1994) Identification and molecular genetic characterization of a sensor kinase responsible for coordinately regulating light harvesting and reaction center gene expression in response to anaerobiosis. J Bacteriol 176:7566–7573
Mouncey NJ, Kaplan S (1998) Oxygen regulation of the ccoN gene encoding a component of the cbb3 oxidase in Rhodobacter sphaeroides 2.4.1 T: involvement of the FnrL protein. J Bacteriol 180:2228–2231
Neidle EL, Kaplan S (1993a) Expression of the Rhodobacter sphaeroides hemA and hemT genes, encoding two 5-aminolevulinic acid synthase isozymes. J Bacteriol 175:2292–2303
Neidle EL, Kaplan S (1993b) 5-Aminolevulinic acid availability and control of spectral complex formation in hemA and hemT mutants of Rhodobacter sphaeroides. J Bacteriol 175:2304–2313
Newman JD, Falkowski MJ, Schilke BA, Anthony LC, Donohue TJ (1999) The Rhodobacter sphaeroides ECF sigma factor, sigma(E), and the target promoters cycA P3 and rpoE P1. J Mol Biol 294:307–320
O’Gara JP, Eraso JM, Kaplan S (1998) A redox-responsive pathway for aerobic regulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1. J Bacteriol 180:4044–4050
Oh JI, Kaplan S (1999) The cbb3 terminal oxidase of Rhodobacter sphaeroides 2.4.1: structural and functional implications for the regulation of spectral complex formation. Biochemistry 38:2688–2696
Oh JI, Kaplan S (2002) Oxygen adaptation. The role of the CcoQ subunit of the cbb3 cytochrome c oxidase of Rhodobacter sphaeroides 2.4.1. J Biol Chem 277:16220–16228
Osman D, Cavet JS (2008) Copper homeostasis in bacteria. Adv Appl Microbiol 65:217–247
Ouchane S, Picaud M, Therizols P, Reiss-Husson F, Astier C (2007) Global regulation of photosynthesis and respiration by FnrL: the first two targets in the tetrapyrrole pathway. J Biol Chem 282:7690–7699
Pawlik G, Kulajta C, Sachelaru I, Schröder S, Waidner B, Hellwig P, Daldal F, Koch H-G (2010) The putative assembly factor CcoH is stably associated with the cbb3-type cytochrome oxidase. J Bacteriol 192:6378–6389
Penfold RJ, Pemberton JM (1991) A gene from the photosynthetic gene cluster of Rhodobacter sphaeroides induces trans suppression of bacteriochlorophyll and carotenoid levels in R. sphaeroides and R. capsulatus. Curr Microbiol 23:259–263
Penfold RJ, Pemberton JM (1994) Sequencing, chromosomal inactivation, and functional expression in Escherichia coli of ppsR, a gene which represses carotenoid and bacteriochlorophyll synthesis in Rhodobacter sphaeroides. J Bacteriol 176:2869–2876
Peters A, Kulajta C, Pawlik G, Daldal F, Koch H-G (2008) Stability of the cbb3-type cytochrome oxidase requires specific CcoQ-CcoP interactions. J Bacteriol 190:5576–5586
Pierre Y, Breyton C, Lemoine Y, Robert B, Vernotte C, Popot JL (1997) On the presence and role of a molecule of chlorophyll a in the cytochrome b 6 f complex. J Biol Chem 272:21901–21908
Ponnampalam SN, Bauer CE (1997) DNA binding characteristics of CrtJ. A redox-responding repressor of bacteriochlorophyll, carotenoid, and light harvesting-II gene expression in Rhodobacter capsulatus. J Biol Chem 272:18391–18396
Ponnampalam SN, Elsen S, Bauer CE (1998) Aerobic repression of the Rhodobacter capsulatus bchC promoter involves cooperative interactions between CrtJ bound to neighboring palindromes. J Biol Chem 273:30757–30761
Pontier D, Albrieux C, Joyard J, Lagrange T, Block MA (2007) Knock-out of the magnesium protoporphyrin IX methyltransferase gene in Arabidopsis. Effects on chloroplast development and on chloroplast-to-nucleus signaling. J Biol Chem 282:2297–2304
Pontoppidan B, Kannangara CG (1994) Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis. Eur J Biochem 225:529–537
Qi Z, O’Brian MR (2002) Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis. Mol Cell 9:155–162
Ranson-Olson B, Zeilstra-Ryalls JH (2008) Regulation of the Rhodobacter sphaeroides 2.4.1 hemA gene by PrrA and FnrL. J Bacteriol 190:6769–6778
Ranson-Olson B, Jones DF, Donohue TJ, Zeilstra-Ryalls JH (2006) In vitro and in vivo analysis of the role of PrrA in Rhodobacter sphaeroides 2.4.1 hemA gene expression. J Bacteriol 188:3208–3218
Reddy VS, Shlykov MA, Castillo R, Sun EI, Saier MH (2012) The major facilitator superfamily (MFS) revisited. FEBS J 279:2022–2035
Rey FE, Harwood CS (2010) FixK, a global regulator of microaerobic growth, controls photosynthesis in Rhodopseudomonas palustris. Mol Microbiol 75:1007–1020
Rieble S, Beale SI (1991) Purification of glutamyl-tRNA reductase from Synechocystis sp. PCC 6803. J Biol Chem 266:9740–9745
Sandström S, Ivanov AG, Park YI, Öquist G, Gustafsson P (2002) Iron stress responses in the cyanobacterium Synechococcus sp. PCC7942. Physiol Plant 116:255–263
Schilke BA, Donohue TJ (1992) delta-Aminolevulinate couples cycA transcription to changes in heme availability in Rhodobacter sphaeroides. J Mol Biol 226:101–115
Schön A, Krupp G, Gough SP, Berry-Lowe S, Kannangara CG, Söll D (1986) The RNA required in the first step of chlorophyll biosynthesis is a chloroplast glutamate tRNA. Nature 322:281–284
Shemin D, Russell CS (1953) δ-Aminolevulinic acid, its role in the biosynthesis of porphyrins and purines. J Am Chem Soc 75:4873–4874
Shi T, Sun Y, Falkowski PG (2007) Effects of iron limitation on the expression of metabolic genes in the marine cyanobacterium Trichodesmium erythraeum IMS101. Environ Microbiol 9:2945–2956
Smart JL, Bauer CE (2006) Tetrapyrrole biosynthesis in Rhodobacter capsulatus is transcriptionally regulated by the heme-binding regulatory protein, HbrL. J Bacteriol 188:1567–1576
Smart JL, Willett JW, Bauer CE (2004) Regulation of hem gene expression in Rhodobacter capsulatus by redox and photosystem regulators RegA, CrtJ, FnrL, and AerR. J Mol Biol 342:1171–1186
Srivastava A, Beale SI (2005) Glutamyl-tRNA reductase of Chlorobium vibrioforme is a dissociable homodimer that contains one tightly bound heme per subunit. J Bacteriol 187:4444–4450
Srivastava A, Lake V, Nogaj LA, Mayer SM, Willows RD, Beale SI (2005) The Chlamydomonas reinhardtii gtr gene encoding the tetrapyrrole biosynthetic enzyme glutamyl-tRNA reductase: structure of the gene and properties of the expressed enzyme. Plant Mol Biol 58:643–658
Suzuki JY, Bollivar DW, Bauer CE (1997) Genetic analysis of chlorophyll biosynthesis. Annu Rev Genet 31:61–89
Swem DL, Bauer CE (2002) Coordination of ubiquinol oxidase and cytochrome cbb(3) oxidase expression by multiple regulators in Rhodobacter capsulatus. J Bacteriol 184:2815–2820
Swem LR, Elsen S, Bird TH, Swem DL, Koch HG, Myllykallio H, Daldal F, Bauer CE (2001) The RegB/RegA two-component regulatory system controls synthesis of photosynthesis and respiratory electron transfer components in Rhodobacter capsulatus. J Mol Biol 309:121–138
Swem LR, Kraft BJ, Swem DL, Setterdahl AT, Masuda S, Knaff DB, Zaleski JM, Bauer CE (2003) Signal transduction by the global regulator RegB is mediated by a redox-active cysteine. EMBO J 22:4699–4708
Swem LR, Gong X, Yu C-A, Bauer CE (2006) Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB. J Biol Chem 281:6768–6775
Thompson AW, Huang K, Saito MA, Chisholm SW (2011) Transcriptome response of high- and low-light-adapted Prochlorococcus strains to changing iron availability. ISME J 5:1580–1594
Tottey S, Rich PR, Rondet SA, Robinson NJ (2001) Two Menkes-type atpases supply copper for photosynthesis in Synechocystis PCC 6803. J Biol Chem 276:19999–20004
Tottey S, Rondet SAM, Borrelly GPM, Robinson PJ, Rich PR, Robinson NJ (2002) A copper metallochaperone for photosynthesis and respiration reveals metal-specific targets, interaction with an importer, and alternative sites for copper acquisition. J Biol Chem 277:5490–5497
Touati D (2000) Iron and oxidative stress in bacteria. Arch Biochem Biophys 373:1–6
Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, …, Yoshikawa S (1995) Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A. Science 269:1069–1074
Vasileuskaya Z, Oster U, Beck CF (2005) Mg-protoporphyrin IX and heme control HEMA, the gene encoding the first specific step of tetrapyrrole biosynthesis, in Chlamydomonas reinhardtii. Eukaryot Cell 4:1620–1628
von Wettstein D, Gough SP, Kannangara CG (1995) Chlorophyll biosynthesis. Plant Cell 7:1039–1057
Voss B, Meinecke L, Kurz T, Al-Babili S, Beck CF, Hess WR (2011) Hemin and magnesium-protoporphyrin IX induce global changes in gene expression in Chlamydomonas reinhardtii. Plant Physiol 155:892–905
Vothknecht UC, Kannangara CG, von Wettstein D (1996) Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase. Proc Natl Acad Sci U S A 93:9287–9291
Wainio WW, Vander Wende C, Shimp NF (1959) Copper in cytochrome C oxidase. J Biol Chem 234:2433–2436
Waldron KJ, Tottey S, Yanagisawa S, Dennison C, Robinson NJ (2007) A periplasmic iron-binding protein contributes toward inward copper supply. J Biol Chem 282:3837–3846
Weinstein JD, Beale SI (1985) Enzymatic conversion of glutamate to delta-aminolevulinate in soluble extracts of the unicellular green alga, Chlorella vulgaris. Arch Biochem Biophys 237:454–464
Willett JW, Smart JL, Bauer CE (2007) RegA control of bacteriochlorophyll and carotenoid synthesis in Rhodobacter capsulatus. J Bacteriol 189:7765–7773
Wu J, Bauer CE (2010) RegB kinase activity is controlled in part by monitoring the ratio of oxidized to reduced ubiquinones in the ubiquinone pool. mBio 1:e00272-10
Wu J, Cheng Z, Reddie K, Carroll K, Hammad LA, Karty JA, Bauer CE (2013) RegB kinase activity is repressed by oxidative formation of cysteine sulfenic acid. J Biol Chem 288:4755–4762
Xiong J, Bauer CE (2002) Complex evolution of photosynthesis. Annu Rev Plant Biol 53:503–521
Xiong J, Fischer WM, Inoue K, Nakahara M, Bauer CE (2000) Molecular evidence for the early evolution of photosynthesis. Science 289:1724–1730
Yin L, Bauer CE (2013) Controlling the delicate balance of tetrapyrrole biosynthesis. Philos Trans R Soc B 368:20120262
Yin L, Dragnea V, Bauer CE (2012) PpsR, a regulator of heme and bacteriochlorophyll biosynthesis, is a heme-sensing protein. J Biol Chem 287:13850–13858
Zappa S, Bauer CE (2013) The LysR-type transcription factor HbrL is a global regulator of iron homeostasis and porphyrin synthesis in Rhodobacter capsulatus. Mol Microbiol 90:1277–1292
Zeilstra-Ryalls JH, Kaplan S (1995) Aerobic and anaerobic regulation in Rhodobacter sphaeroides 2.4.1: the role of the fnrL gene. J Bacteriol 177:6422–6431
Zeilstra-Ryalls JH, Gabbert KK, Mouncey NJ, Kaplan S, Kranz RG (1997) Analysis of the fnrL gene and its function in Rhodobacter capsulatus. J Bacteriol 179:7264–7273
Zhang L, McSpadden B, Pakrasi HB, Whitmarsh J (1992) Copper-mediated regulation of cytochrome c553 and plastocyanin in the cyanobacterium Synechocystis 6803. J Biol Chem 267:19054–19059
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Zappa, S., Bauer, C.E. (2016). Regulating Synthesis of Cytochromes. In: Cramer, W., Kallas, T. (eds) Cytochrome Complexes: Evolution, Structures, Energy Transduction, and Signaling. Advances in Photosynthesis and Respiration, vol 41. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-7481-9_25
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