| http://purl.uniprot.org/citations/15516695 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15516695 | http://www.w3.org/2000/01/rdf-schema#comment | "Heme oxygenase-1 (HO-1) catalyzes the physiological degradation of heme at the expense of molecular oxygen using electrons donated by NADPH-cytochrome P450 reductase (CPR). In this study, we investigated the effect of NADP(H) on the interaction of HO-1 with CPR by surface plasmon resonance. We found that HO-1 associated with CPR more tightly in the presence of NADP(+) (K(D) = 0.5 microm) than in its absence (K(D) = 2.4 microm). The HO-1 mutants, K149A, K149A/K153A, and R185A, showed almost no heme degradation activity with NADPH-CPR, whereas they exhibited activity comparable to that of the wild type when sodium ascorbate was used. R185A showed a 100-fold decreased affinity for CPR compared with wild type, even in the presence of NADP(+) (K(D) = 36.3 microm). The affinities of K149A and K149A/K153A for CPR were decreased 7- and 9-fold (K(D) = 16.8 and 21.8 microm), respectively. In contrast to R185A, the affinities of K149A and K149A/K153A were improved by the addition of NADP(+) (K(D) = 5.2 and 9.6 microm, respectively), as was the case with wild type. Computer modeling of the HO-1/CPR complex showed that the guanidino group of Arg(185) is located within the hydrogen bonding distance of 2'-phosphate of NADPH, suggesting that Arg(185) contributes to the binding to CPR through an electrostatic interaction with the phosphate group. On the other hand, Lys(149) is close to a cluster of acidic amino acids near the FMN binding site of CPR. Thus, Lys(149) and Lys(153) appear to interact with CPR in such a way as to orient the redox partners for optimal electron transfer from FMN of CPR to heme of HO-1."xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m406203200"xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/author | "Fukuyama K."xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/author | "Hayashi S."xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/author | "Sakamoto H."xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/author | "Noguchi M."xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/author | "Palmer G."xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/author | "Higashimoto Y."xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/author | "Sugishima M."xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/pages | "729-737"xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/title | "Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase."xsd:string |
| http://purl.uniprot.org/citations/15516695 | http://purl.uniprot.org/core/volume | "280"xsd:string |
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