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Volumn 46, Issue , 2002, Pages 257-318

Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; COPROPORPHYRINOGEN; COPROPORPHYRINOGEN OXIDASE; CYTOCHROME C; FERROCHELATASE; HEME; HEME DERIVATIVE; IRON; MITOCHONDRIAL ENZYME; OXYGEN; PORPHOBILINOGEN; PORPHOBILINOGEN DEAMINASE; PORPHOBILINOGEN SYNTHASE; PROTOPORPHYRIN; PYRROLE DERIVATIVE; TETRAPYRROLE; UNCLASSIFIED DRUG; UROPORPHYRINOGEN; UROPORPHYRINOGEN DECARBOXYLASE; UROPORPHYRINOGEN III SYNTHASE;

EID: 0035985617     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2911(02)46006-7     Document Type: Review
Times cited : (51)

References (305)
  • 6
    • 0024371112 scopus 로고
    • Identification of the enzymatic basis for δ-aminolevulinic acid auxotrophy in a hemA mutant of Escherichia coli
    • (1989) J. Bacteriol. , vol.171 , pp. 2919-2924
    • Avissar, Y.J.1    Beale, S.I.2
  • 7
    • 0025248423 scopus 로고
    • Cloning and expression of a structural gene from Chlorobium vibrioforme that complements the hemA mutation in Escherichia coli
    • (1990) J. Bacteriol. , vol.172 , pp. 1656-1659
    • Avissar, Y.J.1    Beale, S.I.2
  • 10
    • 0019321415 scopus 로고
    • Formation of an Iso-l-cytochrome c-like species containing a covalently bonded heme group from the apoprotein by a yeast cell-free system in the presence of hemin
    • (1980) J. Biol. Chem. , vol.255 , pp. 7181-7191
    • Basile, G.1    Di Bello, C.2    Taniuchi, H.3
  • 13
    • 0026048393 scopus 로고
    • Purification and spectral characterization of a b-type cytochrome from the plasma membrane of the archaebacterium Sulfolobus acidocaldarius
    • (1991) FEBS Lett. , vol.291 , pp. 331-335
    • Becker, M.1    Schäfer, G.2
  • 18
    • 0025219623 scopus 로고
    • Isolation of a Rhodobacter capsulatus mutant that lacks c-type cytochromes and excretes porphyrins
    • (1990) J. Bacteriol. , vol.172 , pp. 1321-1326
    • Biel, S.W.1    Biel, A.J.2
  • 28
    • 0027432041 scopus 로고
    • Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase is essential for symbiosis with soybean and contains a novel metal-binding domain
    • (1993) J. Bacteriol. , vol.175 , pp. 7222-7227
    • Chauhan, S.1    O'Brian, M.R.2
  • 29
    • 0029121431 scopus 로고
    • A mutant Bradyrhizobium japonicum δ-aminolevulinic acid dehydratase with an altered metal requirement functions in situ for tetrapyrrole synthesis in soybean root nodules
    • (1995) J. Biol. Chem. , vol.270 , pp. 19823-19827
    • Chauhan, S.1    O'Brian, M.R.2
  • 30
    • 0031007110 scopus 로고    scopus 로고
    • Transcriptional regulation of δ-aminolevulinic acid dehydratase synthesis by oxygen in Bradyrhizobium japonicum and evidence for developmental control of the hemB gene
    • (1997) J. Bacteriol. , vol.179 , pp. 3706-3710
    • Chauhan, S.1    O'Brian, M.R.2
  • 33
    • 0034011364 scopus 로고    scopus 로고
    • Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm
    • (2000) Mol. Microbiol. , vol.35 , pp. 1099-1109
    • Chung, J.1    Chen, T.2    Missiakas, D.3
  • 35
    • 0033968656 scopus 로고    scopus 로고
    • Oxidase and periplasmic cytochrome assembly in Escherichia coli K-12: CydDC and CcmAB are not required for haem-membrane association
    • (2000) Microbiology , vol.146 , pp. 527-536
    • Cook, G.M.1    Poole, R.K.2
  • 37
    • 0028930524 scopus 로고
    • The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein. DipZ, with a protein disulphide isomerase-like domain
    • (1995) Mol. Microbiol. , vol.15 , pp. 1139-1150
    • Crooke, H.1    Cole, J.2
  • 39
    • 0029994636 scopus 로고    scopus 로고
    • Protoporphyrinogen oxidase of Myxococcus xanthus-expression, purification and characterization of the cloned enzyme
    • (1996) J. Biol. Chem. , vol.271 , pp. 8714-8718
    • Dailey, H.A.1    Dailey, T.A.2
  • 44
    • 0032577574 scopus 로고    scopus 로고
    • Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases and phytoene desaturase. Expression and characterization of phytoene desaturase of Myxococcus xanthus
    • (1998) J. Biol. Chem. , vol.273 , pp. 13658-13662
    • Dailey, T.A.1    Dailey, H.A.2
  • 45
    • 0027979040 scopus 로고
    • Effect of heme and oxygen availability on hemA gene expression in Escherichia coli: Role of the fnr, arcA, and himA gene products
    • (1994) J. Bacteriol. , vol.176 , pp. 5270-5276
    • Darie, S.1    Gunsalus, R.P.2
  • 57
    • 0024279426 scopus 로고
    • Coupling of heme attachment to import of cytochrome c into yeast mitochondria. Studies with heme lyase-deficient mitochondria and altered apocytochromes c
    • (1988) J. Biol. Chem. , vol.263 , pp. 15928-15937
    • Dumont, M.E.1    Ernst, J.F.2    Sherman, F.3
  • 62
    • 0024384959 scopus 로고
    • Cloning, genetic characterization and nucleotide sequence of the hemA-prfA operon of Salmonella typhimurium
    • (1989) J. Bacteriol. , vol.171 , pp. 3948-3960
    • Elliott, T.1
  • 63
    • 0027446537 scopus 로고
    • Transport of 5-aminolevulinic acid by the dipeptide permease in Salmonella typhimurium
    • (1993) J. Bacteriol. , vol.175 , pp. 325-331
    • Elliott, T.1
  • 88
    • 0025733495 scopus 로고
    • Characterization of a quinol-oxidase activity in crude extracts of Thermoplasma acidophilum and isolation of an 18-kDa cytochrome
    • (1991) Eur. J. Biochem. , vol.200 , pp. 215-222
    • Gartner, P.1
  • 101
    • 0026676696 scopus 로고
    • Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes
    • (1992) J. Bacteriol. , vol.174 , pp. 8081-8093
    • Hansson, M.1    Hederstedt, L.2
  • 105
    • 0019756052 scopus 로고
    • Assembly of cytochrome c. Apocytochrome c is bound to specific sites on mitochondria before its conversion to holocytochrome c
    • (1981) Eur. J. Biochem. , vol.121 , pp. 203-212
    • Hennig, B.1    Neupert, W.2
  • 113
    • 0028835777 scopus 로고
    • Biosynthesis of cytochrome f in Chlamydomonas reinhardtii: Analysis of the pathway in gabaculine-treated cells and in the heme attachment mutant B6
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 156-165
    • Howe, G.1    Mets, L.2    Merchant, S.3
  • 114
    • 0025973280 scopus 로고
    • Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite
    • (1991) J. Bacteriol. , vol.173 , pp. 1544-1553
    • Huang, C.J.1    Barrett, E.L.2
  • 119
    • 0029617402 scopus 로고
    • Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. strain 7. III. The archaeal novel respiratory complex II (succinate: Caldariellaquinone oxidoreductase complex) inherently lacks heme groups
    • (1995) J. Biol. Chem. , vol.270 , pp. 30902-30908
    • Iwasaki, T.1    Wakagi, T.2    Oshima, T.3
  • 123
    • 0021762814 scopus 로고
    • Protoporphyrinogen oxidation, an enzymatic step in heme and chlorophyll synthesis: Partial characterization of the reaction in plant organelles and comparison with mammalian and bacterial systems
    • (1984) Arch. Biochem. Biophys. , vol.229 , pp. 312-319
    • Jacobs, J.M.1    Jacobs, N.J.2
  • 127
  • 134
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 139
    • 0031053298 scopus 로고    scopus 로고
    • Identification of the lrp gene in Bradyrhizobium japonicum and its role in regulation of δ-aminolevulinic acid uptake
    • (1997) J. Bacteriol. , vol.179 , pp. 1828-1831
    • King, N.D.1    O'Brian, M.R.2
  • 141
    • 0023445076 scopus 로고
    • Purification and properties of protoporphyrinogen oxidase from an anaerobic bacterium, Desulfovibrio gigas
    • (1987) J. Bacteriol. , vol.169 , pp. 5209-5215
    • Klemm, D.J.1    Barton, L.L.2
  • 151
    • 0033768478 scopus 로고    scopus 로고
    • Overexpression of plastidic protoporphyrinogen IX oxidase leads to resistance to the diphenyl-ether herbicide acifluorfen
    • (2000) Plant Physiol. , vol.122 , pp. 75-84
    • Lermontova, I.1    Grimm, B.2
  • 158
  • 160
    • 0027473776 scopus 로고
    • Order of uroporphyrinogen III decarboxylation on incubation of porphobilinogen and uroporphyrinogen III with erythrocyte uroporphyrinogen decarboxylase
    • (1993) Biochem. J. , vol.289 , pp. 529-532
    • Luo, J.1    Lim, C.K.2
  • 164
    • 0009381126 scopus 로고
    • Biosynthesis of δ-aminolevulinic acid in Chlamydomonas reinhardtii. Study of the transamination mechanism using specifically labeled glutamate
    • (1988) Plant Physiol. , vol.86 , pp. 793-797
    • Mau, Y.-H.L.1    Wang, W.-Y.2
  • 173
    • 0031007125 scopus 로고    scopus 로고
    • Reduction of uroporphyrinogen decarboxylase by antisense RNA expression affects activities of other enzymes involved in tetrapyrrole biosynthesis and leads to light-dependent necrosis
    • (1997) Plant Physiol. , vol.113 , pp. 1101-1112
    • Mock, H.-P.1    Grimm, B.2
  • 181
    • 0027252484 scopus 로고
    • 5-Aminolevulinic acid availability and control of spectral complex formation in hemA and hemT mutants of Rhodobacter sphaeroides
    • (1993) J. Bacteriol. , vol.175 , pp. 2304-2313
    • Neidle, E.L.1    Kaplan, S.2
  • 182
    • 0027168245 scopus 로고
    • Expression of the Rhodobacter sphaeroides hemA and hemT genes, encoding two 5-aminolevulinic acid synthase isozymes
    • (1993) J. Bacteriol. , vol.175 , pp. 2292-2303
    • Neidle, E.L.1    Kaplan, S.2
  • 193
    • 0029863747 scopus 로고    scopus 로고
    • Heme synthesis in the rhizobium-legume symbiosis: A palette for bacterial and eukaryotic pigments
    • (1996) J. Bacteriol. , vol.178 , pp. 2471-2478
    • O'Brian, M.R.1
  • 196
    • 0035843908 scopus 로고    scopus 로고
    • Genes lost and genes found: Evolution of bacterial pathogenesis and symbiosis
    • (2001) Science , vol.292 , pp. 1096-1098
    • Ochman, H.1    Moran, N.A.2
  • 198
    • 0034034325 scopus 로고    scopus 로고
    • Interacting regulatory circuits involved in orderly control of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1
    • (2000) J. Bacteriol. , vol.182 , pp. 3081-3087
    • Oh, J.I.1    Eraso, J.M.2    Kaplan, S.3
  • 200
    • 0025140710 scopus 로고
    • 1 are translocated to the periplasm of Paracoccus denitrificans in the absence of haem incorporation caused by either mutation or inhibition of haem synthesis
    • (1990) Mol. Microbiol. , vol.4 , pp. 1181-1192
    • Page, M.D.1    Ferguson, S.J.2
  • 212
    • 0034111025 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of the pathway in Pantoea citrea leading to pink disease of pineapple
    • (2000) J. Bacteriol. , vol.182 , pp. 2230-2237
    • Pujol, C.J.1    Kado, C.I.2
  • 213
    • 0036161801 scopus 로고    scopus 로고
    • Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis
    • (2002) Mol. Cell , vol.9 , pp. 155-162
    • Qi, Z.1    O'Brian, M.R.2
  • 228
    • 0028116313 scopus 로고
    • Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein
    • (1994) FEBS Lett. , vol.353 , pp. 235-238
    • Sambongi, Y.1    Ferguson, S.J.2
  • 230
    • 0000892106 scopus 로고
    • Evidence for an inter-organismic heme biosynthetic pathway in symbiotic soybean root nodules
    • (1991) Science , vol.251 , pp. 1220-1222
    • Sangwan, I.1    O'Brian, M.R.2
  • 231
    • 0033080457 scopus 로고    scopus 로고
    • Expression of a soybean gene encoding the tetrapyrrole synthesis enzyme glutamyl-tRNA reductase in symbiotic root nodules
    • (1999) Plant Physiol. , vol.119 , pp. 593-598
    • Sangwan, I.1    O'Brian, M.R.2
  • 239
    • 0030732290 scopus 로고    scopus 로고
    • Transcription of the Corynebacterium diphtheriae hmuO gene is regulated by iron and heme
    • (1997) Infect. Immun. , vol.65 , pp. 4634-4641
    • Schmitt, M.P.1
  • 240
    • 0031034090 scopus 로고    scopus 로고
    • Utilization of host iron sources by Corynebacterium diphtheriae: Identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin
    • (1997) J. Bacteriol. , vol.179 , pp. 838-845
    • Schmitt, M.P.1
  • 241
    • 4243807184 scopus 로고
    • Characterization of the RNA required for biosynthesis of δ-aminolevulinic acid from glutamate. Purification by anticodon-based affinity chromatography and determination that the UUC glutamate anticodon is a general requirement for function in ALA synthesis
    • (1988) Plant Physiol. , vol.86 , pp. 497-504
    • Schneegurt, M.A.1    Beale, S.I.2
  • 244
    • 0034462879 scopus 로고    scopus 로고
    • Interspecies complementation of Escherichia coli ccm mutants: CcmE (CycJ) from Bradyrhizobium japonicum acts as a heme chaperone during cytochrome c maturation
    • (2000) J. Bacteriol. , vol.182 , pp. 6831-6833
    • Schulz, H.1    Thöny-Meyer, L.2
  • 247
    • 0033771110 scopus 로고    scopus 로고
    • New insights into the role of CcmC, CcmD, and CcmE in the haem delivery pathway during cytochrome c maturation by a complete mutational analysis of the conserved tryptophan-rich motif of CcmC
    • (2000) Mol. Microbiol. , vol.37 , pp. 1379-1388
    • Schulz, H.1    Pellicioli, E.2    Thöny-Meyer, L.3
  • 250
    • 0020611838 scopus 로고
    • Anaerobic and aerobic coproporphyrinogen III oxidases of Rhodopseudomonas spheroides. Mechanism and stereochemistry of vinyl group formation
    • (1983) Biochem. J. , vol.209 , pp. 709-718
    • Seehra, J.S.1    Jordan, P.M.2    Akhtar, M.3
  • 257
    • 0033230589 scopus 로고    scopus 로고
    • Six conserved cysteines of the membrane protein DsbD required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
    • (1999) EMBO J. , vol.18 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2    Beckwith, J.3
  • 261
    • 0030054651 scopus 로고    scopus 로고
    • Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation
    • (1996) Biochemistry , vol.35 , pp. 8934-8941
    • Tan, D.1    Ferreira, G.C.2
  • 264
    • 0030953231 scopus 로고    scopus 로고
    • Translocation to the periplasm and signal sequence cleavage of preapocytochrome c depend on sec and lep, but not on the ccm gene products
    • (1997) Eur. J. Biochem. , vol.246 , pp. 794-799
    • Thöny-Meyer, L.1    Künzler, P.2
  • 270
    • 0033527559 scopus 로고    scopus 로고
    • Accumulation of pre-apocytochrome f in a Synechocystis sp. PCC 6803 mutant impaired in cytochrome c maturation
    • (1999) J. Biol. Chem. , vol.274 , pp. 32396-32401
    • Tichy, M.1    Vermaas, W.2
  • 271
    • 0029009423 scopus 로고
    • Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase
    • (1995) J. Bacteriol. , vol.177 , pp. 3326-3331
    • Troup, B.1    Hungerer, C.2    Jahn, D.3
  • 277
    • 0024724030 scopus 로고
    • Isolation, nucleotide sequence and preliminary characterization of the Escherichia coli K-12 hemA gene
    • (1989) J. Bacteriol. , vol.171 , pp. 4728-4735
    • Verkamp, E.1    Chelm, B.K.2
  • 283
    • 0032841896 scopus 로고    scopus 로고
    • A mutant HemA protein with positive charge close to the N terminus is stabilized against heme-regulated proteolysis in Salmonella typhimurium
    • (1999) J. Bacteriol. , vol.181 , pp. 6033-6041
    • Wang, L.1    Wilson, S.2    Elliott, T.3
  • 284
    • 0344361618 scopus 로고    scopus 로고
    • Regulation of heme biosynthesis in Salmonella typhimurium: Activity of glutamyl-tRNA reductase (HemA) is greatly elevated during heme limitation by a mechanism which increases abundance of the protein
    • (1997) J. Bacteriol. , vol.179 , pp. 2907-2914
    • Wang, L.Y.1    Brown, L.2    Elliott, M.3    Elliott, T.4
  • 285
    • 0024285820 scopus 로고
    • Investigation into the nature of substrate binding to the dipyrromethane cofactor of Escherichia coli porphobilinogen deaminase
    • (1988) Biochemistry , vol.27 , pp. 9020-9030
    • Warren, M.J.1    Jordan, P.M.2
  • 287
    • 0021099519 scopus 로고
    • Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis
    • (1983) J. Biol. Chem. , vol.258 , pp. 6799-6807
    • Weinstein, J.D.1    Beale, S.I.2
  • 292
    • 0029867910 scopus 로고    scopus 로고
    • The plastid-encoded ccaA gene is required for heme attachment to chloroplast c-type cytochromes
    • (1996) J. Biochem. , vol.271 , pp. 4632-4639
    • Xie, Z.1    Merchant, S.2
  • 295
    • 0028304529 scopus 로고
    • Cloning, DNA sequence and complementation analysis of the Salmonella typhimurium hemN gene encoding a putative oxygen-independent coproporphyrinogen III oxidase
    • (1994) J. Bacteriol. , vol.176 , pp. 3196-3203
    • Xu, K.1    Elliott, T.2
  • 296
    • 0026688997 scopus 로고
    • The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation
    • (1992) J. Bacteriol. , vol.174 , pp. 3953-3963
    • Xu, K.1    Delling, J.2    Elliott, T.3
  • 299
    • 0033597927 scopus 로고    scopus 로고
    • A novel mechanism for the regulation of photosynthesis gene expression by the TspO outer membrane protein of Rhodobacter sphaeroides 2.4.1
    • (1999) J. Biol. Chem. , vol.274 , pp. 21234-21243
    • Yeliseev, A.A.1    Kaplan, S.2


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