Regular ArticlePyrroloquinoline Quinone Acts with Flavin Reductase to Reduce Ferryl Myoglobin in Vitro and Protects Isolated Heart from Reoxygenation Injury
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Myoglobin promotes nitrite-dependent mitochondrial S-nitrosation to mediate cytoprotection after hypoxia/reoxygenation
2020, Nitric Oxide - Biology and ChemistryIn silico and crystallographic studies identify key structural features of biliverdin IX reductase inhibitors having nanomolar potency
2018, Journal of Biological ChemistryCitation Excerpt :In humans, biliverdin reductase IXα (BLVRA) (10–12) effectively reduces BV IXα with less efficient utilization of BV IXβ, IXγ, or IXδ (13). In contrast, biliverdin IXβ reductase (BLVRB) is promiscuous (14, 15), catalyzing the NAD(P)H-dependent reduction of non-IXα biliverdin isomers (IXβ, IXγ, and IXδ) (16), and several flavins, including flavin mononucleotide (FMN) (17), pyrroloquinoline quinone (18), dichlorophenolindophenol (DCPIP), and ferric ion (Fig. 1a) (18). A single dinucleotide-binding domain accommodates both NADPH (or NADH) and substrate(s) within the verdin/flavin (V/F) binding pocket, with no evidence to date for structural or preferred partitioning for either substrate.
Ultrasensitive determination of pyrroloquinoline quinone in human plasma by HPLC with chemiluminescence detection using the redox cycle of quinone
2017, Journal of Pharmaceutical and Biomedical AnalysisCitation Excerpt :Pyrroloquinoline quinone (PQQ, 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylic acid) is a cofactor for methanol dehydrogenase [1] and is categorized as a member of the vitamin B family [2]. PQQ plays important roles in mammals, including protection against liver [3], heart [4], and brain injuries [5], enhancement of the synthesis of DNA in human fibroblasts [6], and promotion of the production of the nerve growth factor [7]. In addition, it has a defensive effect against embryonic cataract induced by hydrocortisone [8] and acts as a radical scavenger [9,10].
Reperfusion injury and reactive oxygen species: The evolution of a concept
2015, Redox BiologyCitation Excerpt :The oxidative stress elicited in tissues/cells following I/R (or H/R) has been linked to a variety of different sources of ROS. Non-enzymatic sources of ROS, such as hemoglobin and myoglobin (both of which can be released into extracellular fluid after trauma), have received some attention as potential mediators of I/R-induced oxidative stress [115,116]. However, most studies have attributed the accelerated ROS production in post-ischemic tissues to one or more enzymes that are capable of reducing molecular oxygen to form superoxide and/or hydrogen peroxide, with the subsequent release of ROS into the intracellular and/or extracellular compartments.
Biosynthesis and Biological Functions of Bilins
2012, The Porphyrin Handbook: Chlorophylls and Bilins: Biosynthesis, Synthesis and Degradation