KEGG   ENZYME: 1.10.9.1Help
Entry
EC 1.10.9.1                 Enzyme                                 

Name
plastoquinol---plastocyanin reductase;
plastoquinol/plastocyanin oxidoreductase;
cytochrome f/b6 complex;
cytochrome b6f complex
Class
Oxidoreductases;
Acting on diphenols and related substances as donors;
With a copper protein as acceptor
BRITE hierarchy
Sysname
plastoquinol:oxidized-plastocyanin oxidoreductase
Reaction(IUBMB)
plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1] = plastoquinone + 2 reduced plastocyanin + 4 H+[side 2] [RN:R03817]
Reaction(KEGG)
R03817;
(other) R08409
Show
Substrate
plastoquinol [CPD:C16693];
oxidized plastocyanin [CPD:C03162];
H+[side 1]
Product
plastoquinone [CPD:C02061];
reduced plastocyanin [CPD:C03025];
H+[side 2]
Comment
Contains two b-type cytochromes, two c-type cytochromes (cn and f), and a [2Fe-2S] Rieske cluster. The enzyme plays a key role in photosynthesis, transferring electrons from photosystem II (EC 1.10.3.9) to photosystem I (EC 1.97.1.12). Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly. In chloroplasts, protons are translocated through the thylakoid membrane from the stroma to the lumen. The mechanism occurs through the Q cycle as in EC 1.10.2.2, quinol---cytochrome-c reductase (complex III) and involves electron bifurcation.
History
EC 1.10.9.1 created 1984 as EC 1.10.99.1, transferred 2011 to EC 1.10.9.1
Pathway
ec00195  Photosynthesis
Orthology
K02636  cytochrome b6-f complex iron-sulfur subunit
Genes
ATH: AT4G03280(PETC)
ALY: ARALYDRAFT_490231
CRB: 17882819
CSAT: 104707757 104715172 104738479
EUS: EUTSA_v10028941mg
BRP: 103846718 103858708
BNA: 106389955 106392303 106401343 106431526 106438729
BOE: 106315451 106328732
THJ: 104801189
CPAP: 110817023
CIT: 102606718
TCC: 18608589
GMX: 100127419(PETC) 100799420
VRA: 106754175
VAR: 108332507
CCAJ: 109806045
CAM: 101497453
LJA: Lj3g3v2742950.1(Lj3g3v2742950.1)
FVE: 101297120
PPER: 18782385
PMUM: 103329498
PAVI: 110772253
CSV: 101221828(PetC)
CMO: 103495550
MCHA: 111008042
RCU: 8287590
JCU: 105633441
HBR: 110656423
JRE: 109014063
SLY: 101243864
SPEN: 107007225
SOT: 102577449(FES)
CANN: 107863280
NTA: 107765416(petC) 107805497(petC2)
NSY: 104226732
NTO: 104089639
INI: 109184540
DCR: 108214328
BVG: 104903038
SOE: 110796530
NNU: 104612240
OSA: 4343570
DOSA: Os07t0556200-01(Os07g0556200)
OBR: 102722030
BDI: 100821378
ATS: 109739965(LOC109739965) 109787183(LOC109787183)
SBI: 8058472
ZMA: 100273026 100273354(ris2)
SITA: 101778821
PDA: 103723659
EGU: 105049872
MUS: 103998870
DCT: 110107309
AOF: 109833255
ATR: 18426417
CRE: CHLREDRAFT_193296(PETC)
VCN: VOLCADRAFT_109628(gon9)
MNG: MNEG_2391
OLU: OSTLU_40083(PETC)
MIS: MICPUN_88922(PETC)
MPP: MICPUCDRAFT_36185(PETC)
APRO: F751_5172
SMIN: v1.2.006093.t1(symbB.v1.2.006093.t1) v1.2.006094.t1(symbB.v1.2.006094.t1) v1.2.006095.t1(symbB.v1.2.006095.t1) v1.2.018676.t1(symbB.v1.2.018676.t1) v1.2.018676.t2(symbB.v1.2.018676.t2) v1.2.035696.t2(symbB.v1.2.035696.t2)
GTT: GUITHDRAFT_183242(PetC)
GSK: KN400_1672(cbcV)
GEB: GM18_0922
DEU: DBW_2723
DOL: Dole_0192
SCL: sce0366
BMX: BMS_0207
STH: STH3146
DSY: DSY0257
DHD: Dhaf_0205
HMO: HM1_0699(petC)
LPIL: LIP_1511
SYN: sll1182(petC) sll1316(petC) slr1185(petC)
SYZ: MYO_110630(petC) MYO_117060(petC) MYO_131630(petC)
SYY: SYNGTS_1054(petC) SYNGTS_1688(petC) SYNGTS_3127(petC)
SYT: SYNGTI_1054(petC) SYNGTI_1688(petC) SYNGTI_3126(petC)
SYS: SYNPCCN_1053(petC) SYNPCCN_1687(petC) SYNPCCN_3125(petC)
SYQ: SYNPCCP_1053(petC) SYNPCCP_1687(petC) SYNPCCP_3125(petC)
SYJ: D082_26430(petC1) D082_33580(petC3)
SYW: SYNW1841(petC)
SYC: syc0318_d(petC)
SYG: sync_2149(petC)
SYR: SynRCC307_0704(petC)
SYX: SynWH7803_1850(petC)
SYP: SYNPCC7002_A1909(petC) SYNPCC7002_G0076(petC-II)
CYA: CYA_1403(petC)
CYB: CYB_1622(petC)
SYNR: KR49_12220
SYND: KR52_13850
SYH: Syncc8109_0687(petC)
SYNW: SynWH8103_02096(petC)
TEL: tlr0959(petC)
THN: NK55_11380(petC)
CYI: CBM981_1275(petC)
LET: O77CONTIG1_03342(petC_1) O77CONTIG1_03479(petC_2)
HHG: XM38_024430(petC_1) XM38_031430(petC_2) XM38_043580(petC_3) XM38_045840(petC_4)
PMA: Pro_0460(petC)
PMM: PMM0462(petC)
PMT: PMT_1322
PMB: A9601_05181(petC)
PMC: P9515_05261(petC)
PMF: P9303_06651(petC)
PMG: P9301_04871(petC)
PMH: P9215_05421(petC)
PMJ: P9211_04631(petC)
PME: NATL1_05171(petC)
PRC: EW14_0505
PRM: EW15_0557
MAR: MAE_19220(petC1) MAE_29060(petC2)
MPK: VL20_5284
CYL: AA637_03160(petC)
CYT: cce_2958(petC1) cce_3410(petC2)
TER: Tery_1799
ARP: NIES39_L01870(petC)
GVI: gvip416(petC)
GLJ: GKIL_0313(petC) GKIL_0990
ANA: all0606(petC) all1512(petC) all2453(petC) all4511(petC)
ANB: ANA_C10614(petC1) ANA_C13772(petC2)
NSP: BMF81_02901(petC) BMF81_03752(petC_2)
CEO: ETSB_0201(petC)
HAU: Haur_4253
PNL: PNK_0024
WCH: wcw_1968
PSL: Psta_2937
PLS: VT03_28950(petC_2)
FMR: Fuma_03692(petC_2)
TTF: THTE_1161
KST: KSMBR1_1275(petC) KSMBR1_3797(qcrB_2)
SUS: Acid_4388
SLI: Slin_4885
ZPR: ZPR_4052
CTE: CT0302(petC)
CPC: Cpar_1735
CCH: Cag_0394
CLI: Clim_0361
PVI: Cvib_1501
PLT: Plut_1719
PPH: Ppha_0466
PAA: Paes_1780
PROC: Ptc2401_01878(petC_2)
CTS: Ctha_0474
MRO: MROS_1771
NJA: NSJP_2410
LFC: LFE_0697
MOX: DAMO_0820 DAMO_1672(petC)
TUZ: TUZN_1070
 » show all
Taxonomy
Reference
1  [PMID:6269845]
  Authors
Hurt E, Hauska G.
  Title
A cytochrome f/b6 complex of five polypeptides with plastoquinol-plastocyanin-oxidoreductase activity from spinach chloroplasts.
  Journal
Eur J Biochem 117:591-5 (1981)
DOI:10.1111/j.1432-1033.1981.tb06379.x
Reference
2  [PMID:16787635]
  Authors
Cramer WA, Zhang H
  Title
Consequences of the structure of the cytochrome b6f complex for its charge transfer pathways.
  Journal
Biochim Biophys Acta 1757:339-45 (2006)
DOI:10.1016/j.bbabio.2006.04.020
Other DBs
ExplorEnz - The Enzyme Database: 1.10.9.1
IUBMB Enzyme Nomenclature: 1.10.9.1
ExPASy - ENZYME nomenclature database: 1.10.9.1
BRENDA, the Enzyme Database: 1.10.9.1
CAS: 79079-13-3

DBGET integrated database retrieval system