Resolution of two native monomeric 90kDa nitrate reductase active proteins from Shewanella gelidimarina and the sequence of two napA genes

Simpson, P.; McKinzie, Audra A.; Codd, Rachel

doi:10.1016/j.bbrc.2010.06.002

Cited by 14 publications

(19 citation statements)

References 25 publications

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“…In a recent study of NapA from Shewanella gelidimarina, the authors proposed that only two of those residues (Glu47 and Ser772 using C. necator numbering) should be crucial for heterodimer stabilization. 31 However, upon analysis of the structure interfaces of CnNapAB and RsNapAB, it appears more likely that the stability of the NapAB heterodimer-and therefore the preservation of its integrity upon purification-is due to a combination of multiple intersubunit interactions. Analyzing for the presence of some of these residues might help in predicting whether a certain Nap protein is expected to isolate as a NapA monomer or as a NapAB heterodimer.…”

Section: Comparison With Homologous Crystal Structuresmentioning

confidence: 98%

The Crystal Structure of Cupriavidus necator Nitrate Reductase in Oxidized and Partially Reduced States

Coelho

González

Moura

et al. 2011

Journal of Molecular Biology

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Section: Comparison With Homologous Crystal Structuresmentioning

confidence: 98%

The Crystal Structure of Cupriavidus necator Nitrate Reductase in Oxidized and Partially Reduced States

Coelho

González

Moura

et al. 2011

Journal of Molecular Biology

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“…This article contains supporting information ( 73 , 74 , 75 , 76 , 77 , 78 , 79 , 80 , 81 , 82 , 83 , 84 , 85 , 86 , 87 ).…”

Section: Supporting Informationmentioning

confidence: 99%

Identification and characterization of a noncanonical menaquinone-linked formate dehydrogenase

Arias-Cartin

Uzel

Seduk

et al. 2022

Journal of Biological Chemistry

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The molybdenum/tungsten— bis -pyranopterin guanine dinucleotide family of formate dehydrogenases (FDHs) plays roles in several metabolic pathways ranging from carbon fixation to energy harvesting because of their reaction with a wide variety of redox partners. Indeed, this metabolic plasticity results from the diverse structures, cofactor content, and substrates used by partner subunits interacting with the catalytic hub. Here, we unveiled two noncanonical FDHs in Bacillus subtilis , which are organized into two-subunit complexes with unique features, ForCE1 and ForCE2. We show that the formate oxidoreductase catalytic subunit interacts with an unprecedented partner subunit, formate oxidoreductase essential subunit, and that its amino acid sequence within the active site deviates from the consensus residues typically associated with FDH activity, as a histidine residue is naturally substituted with a glutamine. The formate oxidoreductase essential subunit mediates the utilization of menaquinone as an electron acceptor as shown by the formate:menadione oxidoreductase activity of both enzymes, their copurification with menaquinone, and the distinctive detection of a protein-bound neutral menasemiquinone radical by multifrequency electron paramagnetic resonance (EPR) experiments on the purified enzymes. Moreover, EPR characterization of both FDHs reveals the presence of several [Fe-S] clusters with distinct relaxation properties and a weakly anisotropic Mo(V) EPR signature, consistent with the characteristic molybdenum/bis-pyranopterin guanine dinucleotide cofactor of this enzyme family. Altogether, this work enlarges our knowledge of the FDH family by identifying a noncanonical FDH, which differs in terms of architecture, amino acid conservation around the molybdenum cofactor, and reactivity.

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“…This could explain why the E. coli NapA was isolated as a monomer, while the R. sphaeroides homologue was isolated as a heterodimer. 254 …”

Section: Periplasmic Nitrate Reductasementioning

confidence: 99%

“…282 The Nap from two operons have been isolated and characterized, and one of them (Nap-α) was found to be more stable. 254 Jepson et al , based on their examination of gene order in 19 Shewanella species, postulated that the different isoforms might serve different functions and/or could be under different regulatory control. 254 However, a closer look at not just the presence of the two isoforms, but the actual number of genes in the operons reveals another more fascinating phenomenon.…”

Section: Periplasmic Nitrate Reductasementioning

confidence: 99%

“…254 Jepson et al , based on their examination of gene order in 19 Shewanella species, postulated that the different isoforms might serve different functions and/or could be under different regulatory control. 254 However, a closer look at not just the presence of the two isoforms, but the actual number of genes in the operons reveals another more fascinating phenomenon. Table 7 shows the gene orders for a total of 26 strains representing 19 species of Shewanella .…”

Section: Periplasmic Nitrate Reductasementioning

confidence: 99%

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Nitrate and periplasmic nitrate reductases

2014

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The nitrate anion is a simple, abundant and relatively stable species, yet plays a significant role in global cycling of nitrogen, global climate change, and human health. Although it has been known for quite some time that nitrate is an important species environmentally, recent studies have identified potential medical applications. In this respect the nitrate anion remains an enigmatic species that promises to offer exciting science in years to come. Many bacteria readily reduce nitrate to nitrite via nitrate reductases. Classified into three distinct types – periplasmic nitrate reductase (Nap), respiratory nitrate reductase (Nar) and assimilatory nitrate reductase (Nas), they are defined by their cellular location, operon organization and active site structure. Of these, Nap proteins are the focus of this review. Despite similarities in the catalytic and spectroscopic properties Nap from different Proteobacteria are phylogenetically distinct. This review has two major sections: in the first section, nitrate in the nitrogen cycle and human health, taxonomy of nitrate reductases, assimilatory and dissimilatory nitrate reduction, cellular locations of nitrate reductases, structural and redox chemistry are discussed. The second section focuses on the features of periplasmic nitrate reductase where the catalytic subunit of the Nap and its kinetic properties, auxiliary Nap proteins, operon structure and phylogenetic relationships are discussed.

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Resolution of two native monomeric 90kDa nitrate reductase active proteins from Shewanella gelidimarina and the sequence of two napA genes

Cited by 14 publications

References 25 publications

The Crystal Structure of Cupriavidus necator Nitrate Reductase in Oxidized and Partially Reduced States

The Crystal Structure of Cupriavidus necator Nitrate Reductase in Oxidized and Partially Reduced States

Identification and characterization of a noncanonical menaquinone-linked formate dehydrogenase

Nitrate and periplasmic nitrate reductases

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