The FNR modules contribute to control nitric oxide synthase catalysis revealed by chimera enzymes

Wang,Ruiqiang; Wang,Biyue; Zheng,Bowen; Ma,Pupu; Gou,Rong; Guo,Yuanyuan; Chen,Fengmei; Li,Hua; Wang,Yi; Pu,Juanjuan; Tang,Lin

doi:10.3892/mmr.2017.7745

The FNR modules contribute to control nitric oxide synthase catalysis revealed by chimera enzymes

Authors:
- Ruiqiang Wang
- Biyue Wang
- Bowen Zheng
- Pupu Ma
- Rong Gou
- Yuanyuan Guo
- Fengmei Chen
- Hua Li
- Yi Wang
- Juanjuan Pu
- Lin Tang
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Affiliations: Department of Nephrology, The First Affiliated Hospital of Zhengzhou University, Zhengzhou, Henan 450052, P.R. China, Department of Gerontology, The First Affiliated Hospital of Zhengzhou University, Zhengzhou, Henan 450052, P.R. China
Published online on: October 9, 2017 https://doi.org/10.3892/mmr.2017.7745
Pages: 9263-9269

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Abstract

The reductase domains of neuronal NOS, endothelial NOS and two constitutive nitric oxide synthase (cNOS) share higher sequence similarity (>60%). In order to evaluate the role of ferredoxin‑NADP+ reductase (FNR) module in adjusting NOS catalytic activities, chimeras were by interchanging the FNR‑like module between endothelial NOS and neuronal NOS in the present study. The assays of steady‑state enzymatic activities for cytochrome c and ferricyanide reduction, NO synthesis and NADPH oxidation were performed spectrophotometrically. The two NOS FNR modules transferred their ferricyanide reductase character to the chimera enzymes. Results showed that the FNR module was important in adjusting electrons flow through the reductase domain and out of the FMN module. Results indicated that the FNR module was critical in controlling the electron transfer capacities of the FMN module.

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