96 resultados para Xanthophyll cycle Mehler-peroxidase reaction
em Chinese Academy of Sciences Institutional Repositories Grid Portal
Resumo:
(ABA)(Pn)(C02)(CE)II (PSII)(PSII)ABAPSII(Fv/Fm)1025mol L-I ABA750mol L-1ABA25mol L-lABAABAPnCEPS II(qP)(NPQ)(qm)Fv/FmABAPsnABA(V)(A)(Z)(V+A+Z)ABAABAPsIIPn(SOD)(APX)(DHAR)(GR)(AsA)(DHAsA)(GSH)(GSSH)ABAMehler-peroxidase III(300molm-2 S-l)655nm700-770 nmI(PSI)II(PSII)1Psn( Fml)PSII( Frri2)20nunPsn2l2PSIIDTTPsII( Fv/Fm)PSII(F0')20minPSIIPSII(B)PSI(a)ABA7PSII(Fm2)Fm1/Fm21-1ABA(qm)NEMABAqm12ABA77KF684/F732ABA 25mol L-l ABA7LT1STC02PsIILTST( Fv/Fm)(CE)(Pn)(Gs)LTST1500mol m-2 s-1Fv/FmLTFv/Fm60minSTFv/FmPS IIPnCELTLT(NPQ)MDASTNPQMDASTLTABAC02
Resumo:
pHzeaxanthin;Zantheraxanthin;AViolaxanthin de-epoxidase;VDEviolaxanthin(A)(Z) VDEpCAMBIA1301TvdepCBTOpCBTA(Agrobacterium tumefaciens)(Nicotiana tabacum L.)PCRhptSouthernTvde1VDEVDE60%VDE75%HPLCZDESNPQFv/FmVDE
Resumo:
41154 1. 41154DCPIP 2. 54F683411 3. 411LHCII54LHCII54 4. SDS-PAGEPSII23kD17kD41123kD17kD5423kD17kD54PSII27kD41127kD 5. 54411 6. 41154VDE 7. 54VAZPSIILHCIILHCIIVAZPSII 8. 54 9. 54
Resumo:
UV-BUV-BUV-BUV-BUV-BUV-B (Triticum aestivum)4.2 kJ m-2 d-1 UV-BBELUVB7.0 kJ m-2 d-1 UV-BBEHUVBUV-B20/16;25/2010/54.2 kJ m-2 d-1 UV-BBELUVB10.3 kJ m-2 d-1 UV-BBESHUVBUV-BUV-B 1.LUVB20/1625/20LT50HUVB20/16LT50SHUVB25/20LT50LUVBSHUVB10/5LT50UV-B20/1625/2010/5UV-B 2.20/16UV-B-66 h6 hUV-BCATGPXGRGSH/GSSGTBARSUV-BH2O2UV-BH2O2UV-B 3.25/20LUVBUV-BRGRPnIIFv/FmII(FmFs)/FmqPUV-BCO2CiUV-BUV-BPS II 4.UV-B20/1625/20VVZLUVBDEPSNPQSHUVBDEPSNPQUV-B 5.UV-B25/20SODAPXGRAsA/DHAGSH/GSSG;10/5UV-BSODCATAPXAsA/DHAGPXGSH/GSSGUV-B10/5 6.UV-B10/5UV-BUV-B 7.SHUVBTBARS10/5UV-BUV-B10/5UV-B
Resumo:
Prunus persica (L.) Batch.PnPngsECiVPDlTlIIPSIICEPnPnPSIIPSIIPSIISODAPXMDARDHARAsAGSHH2O2MDA Malus domestica Borkh.Pn-1,5-/RubiscoIIPSIIPsbAPsbOPngsECiTlPSIIPSIIPSIIRubiscoPSIIPsbAPsbOPn
Resumo:
It was found that at neutral pH the hydroxylation reaction rate of phenol was accelerated with an increase of the amounts of 1,4-quinone (1,4-BQ), This acceleration was ascribed to the formation of semiquinone from 1,4-BQ. The semiquinone and 1,4-BQ were suggested to play a role of actual oxidant (electron transfer) in the catalytic cycle. With further reaction, most 1,4-BQ was converted into 1,4-hydroquinone (HQ) and the corresponding mechanism was proposed.
Resumo:
In this paper, the interaction mechanism between La3+ and microperoxidase-11 (MP-11) in the imitated physiological solution was investigated with the electrochemical and spectroscopic methods. It was found that when the molar ratio of La3+, and MP-11 is low, such as 2, La3+ can coordinate with oxygen in the propionic acid group of the heme group in the MP-11 molecule, forming the La-MP-11 complexes and leading to the increase in the non-planarity of the porphyrin cycle in the heme group and then the increase in the extent of exposure of the electrochemically active center, Fe(I I I) in the porphyrin cycle of the heme group. The increase in the extent of exposure of the electrochemically active center, Fe(III) in the porphyrin cycle of the heme group would increase the reversibility of the electrochemical reaction of the La-MP-11 complexes and its electrocatalytic activity for the reduction of H2O2. The results of the chromatographic analysis demonstrated that the average molar ratio of La3+ and MP-11 in the La-MP-11 complexes is 1.62.When the molar ratio of La3+ and MP-11 is high, such as 3, La3+ would shear some amino acid residues of the peptide of MP-11. Therefore, many La3+ ions can bind to the oxygen- and/or nitrogen-containing groups in the sheared amino acid residues except coordinating with the sheared and non-sheared MP-11 molecules.
Resumo:
It is reported for the first time that horseradish peroxidase (HRP) immobilized on the active carbon can undergo a direct quasi-reversible electrochemical reaction. In addition, the immobilized HRP showed the stable bioelectrocatalytic activity for the reduction of H2O2.
