A new catalytic mechanism of bacterial ferredoxin-NADP⁺ reductases due to a particular NADP⁺ binding mode.

ABSTRACT: Ferredoxin-NADP⁺ reductases (FNRs) are ubiquitous flavoenzymes involved in redox metabolisms. FNRs catalyze the reversible electron transfer between NADP(H) and ferredoxin or flavodoxin. They are classified as plant- and mitochondrial-type FNR. Plant-type FNRs are divided into plastidic and bacterial classes. The plastidic FNRs show turnover numbers between 20 and 100 times higher than bacterial enzymes and these differences have been related to their physiological functions. We demonstrated that purified Escherichia coli FPR (EcFPR) contains tightly bound NADP⁺ , which does not occur in plastidic type FNRs. The three-dimensional structure of EcFPR evidenced that NADP⁺ interacts with three arginines (R144, R174, and R184) which could generate a very high af

SUBMITTER: Monchietti P 

PROVIDER: S-EPMC8442965 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature