Connick, J. Patrick et al. published their research in Biochemical Journal in 2021 |CAS: 55779-48-1

The Article related to heteromeric complex human cytochrome p450 cyp1a1 heme oxygenase, bioluminescence resonance energy transfer, cytochrome p450, heme oxygenase-1, membrane proteins, nadph-cytochrome p450 reductase, protein–protein interactions and other aspects.Formula: C26H21N3O3

On January 31, 2021, Connick, J. Patrick; Reed, James R.; Cawley, George F.; Backes, Wayne L. published an article.Formula: C26H21N3O3 The title of the article was Heteromeric complex formation between human cytochrome P450 CYP1A1 and heme oxygenase-1. And the article contained the following:

P 450 and heme oxygenase-1 (HO-1) receive their necessary electrons by interaction with the NADPH-cytochrome P 450 reductase (POR). As the POR concentration is limiting when compared with P 450 and HO-1, they must effectively compete for POR to function. In addition to these functionally required protein-protein interactions, HO-1 forms homomeric complexes, and several P450s have been shown to form complexes with themselves and with other P450s, raising the question, ‘How are the HO-1 and P 450 systems organized in the endoplasmic reticulum’. Recently, CYP1A2 was shown to associate with HO-1 affecting the function of both proteins. The goal of this study was to determine if CYP1A1 formed complexes with HO-1 in a similar manner. Complex formation among POR, HO-1, and CYP1A1 was measured using bioluminescence resonance energy transfer, with results showing HO-1 and CYP1A1 form a stable complex that was further stabilized in the presence of POR. The POR•CYP1A1 complex was readily disrupted by the addition of HO-1. CYP1A1 also was able to affect the POR•HO-1 complex, although the effect was smaller. This interaction between CYP1A1 and HO-1 also affected function, where the presence of CYP1A1 inhibited HO-1-mediated bilirubin formation by increasing the KPOR•HO-1m without affecting the Vappmax. In like manner, HO-1 inhibited CYP1A1-mediated 7-ethoxyresorufin dealkylation by increasing the KPOR•CYP1A1m. Based on the math. simulation, the results could not be explained by a model where CYP1A1 and HO-1 simply compete for POR, and are consistent with the formation of a stable CYP1A1•HO-1 complex that affected the functional characteristics of both moieties. The experimental process involved the reaction of 8-Benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one(cas: 55779-48-1).Formula: C26H21N3O3

The Article related to heteromeric complex human cytochrome p450 cyp1a1 heme oxygenase, bioluminescence resonance energy transfer, cytochrome p450, heme oxygenase-1, membrane proteins, nadph-cytochrome p450 reductase, protein–protein interactions and other aspects.Formula: C26H21N3O3

Referemce:
Pyrazine – Wikipedia,
Pyrazine | C4H4N2 – PubChem