Effect of Metal Ions on the Activity of Ten NAD-Dependent Formate Dehydrogenases.


Journal

The protein journal
ISSN: 1875-8355
Titre abrégé: Protein J
Pays: Netherlands
ID NLM: 101212092

Informations de publication

Date de publication:
10 2020
Historique:
accepted: 01 10 2020
pubmed: 13 10 2020
medline: 4 2 2021
entrez: 12 10 2020
Statut: ppublish

Résumé

NAD-dependent formate dehydrogenase (FDH) enzymes are frequently used in industrial and scientific applications. FDH is a reversible enzyme that reduces the NAD molecule to NADH and produces CO

Identifiants

pubmed: 33043425
doi: 10.1007/s10930-020-09924-x
pii: 10.1007/s10930-020-09924-x
doi:

Substances chimiques

Bacterial Proteins 0
Fungal Proteins 0
Metals 0
Formate Dehydrogenases EC 1.17.1.9

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

519-530

Références

Zhushan F, Shuhua X (2020) The effects of heavy metals on human metabolism. Toxicol Mech Methods 30:3
Popov VO and Lamzin V. S (1994) NAD+-dependent formate dehydrogenase. Biochem J 301:625–643
doi: 10.1042/bj3010625
Tishkov VI and Popov V. O (2006) Protein engineering of formate dehydrogenase. Biomol Eng 23:89–110
doi: 10.1016/j.bioeng.2006.02.003
Altinkaynak C, Gulmez C, Atakisi O, Özdemir N (2020) Evaluation of organic-inorganic hybrid nanoflower’s enzymatic activity in the presence of different metal ions and organic solvents. Int J Biol Macromol 164:162–171
doi: 10.1016/j.ijbiomac.2020.07.118
Ballinger P, Long FA (1960) Acid Ionization Constants of Alcohols. II. Acidities of Some Substituted Methanols and Related Compounds. J Am Chem Soc 82:795–798
doi: 10.1021/ja01489a008
Tishkov VI and Popov V. O (2004) Catalytic mechanism and application of formate dehydrogenase. Biochemistry 69:1252–1267
pubmed: 15627379
Choe H, Joo JC, Cho DH, Kim MH, Lee SH, Jung KD, Kim YH (2014) Efficient CO2-reducing activity of NAD-dependent formate dehydrogenase from Thiobacillus sp. KNK65MA for formate production from CO2 gas. PLoS One 25(7):e103111 9(
doi: 10.1371/journal.pone.0103111
Jayathilake BS, Bhattacharya S, Vaidehi N, Narayanan SR (2019) Efficient and Selective Electrochemically Driven Enzyme-Catalyzed Reduction of Carbon Dioxide to Formate using Formate Dehydrogenase and an Artificial Cofactor. Acc Chem Res 52:676–685
doi: 10.1021/acs.accounts.8b00551
Aslan AS, Valjakka J, Ruupunen J, Yildirim D, Turner NJ, Turunen O, Binay B (2017) Chaetomium thermophilum formate dehydrogenase has high activity in the reduction of hydrogen carbonate (HCO3–) to formate. Protein Eng Des Sel 30:47–55
pubmed: 27887026
Pietzke M, Meiser J, Vazquez A (2020) Formate metabolism in health and disease. Molecular Metabolism 33:23–37
doi: 10.1016/j.molmet.2019.05.012
Hovda KE, Urdal P, Jacobsen D (2005) Increased serum formate in the diagnosis of methanol poisoning. J Anal Toxicol 29:586–588
doi: 10.1093/jat/29.6.586
Hantson P, Haufroid V, Wallemacq P (2005) Formate kinetics in methanol poisoning. Hum Exp Toxicol. 24(2):55–9
doi: 10.1191/0960327105ht503oa
Onyekwere N, Nwadiuto I, Maleghemi S, Maduka O, Numbere TW, Akpuh N, Kanu E, Katchy I, Okeafor I (2018) Methanol poisoning in South-South Nigeria: Reflections on the outbreak response. J Public Health Africa 9:49–53
Goldberg SL, Nanduri VB, Chu L, Johnston RM, Patel RN (2006) Enantioselective microbial reduction of 6-oxo-8-[4-[4-(2-pyrimidinyl)-1- piperazinyl]butyl]-8-azaspiro[4.5]decane-7,9-dione. Tetrahedron Asymmetry 16:2778–2783
Coleman JS, Gaydos CA, Witter F (2013) Trichomonas vaginalis vaginitis in obstetrics and gynecology practice: New concepts and controversies. Obstet Gynecol Surv 68:43–50
doi: 10.1097/OGX.0b013e318279fb7d
Janson JC (2012) Protein Purification: Principles, High Resolution Methods, and Applications. John Wiley and Sons
Altas N, Aslan AS, Karatas E, Chronopoulou E, Labrou NE, Binay B (2017) Heterologous production of extreme alkaline thermostable NAD+-dependent formate dehydrogenase with wide-range pH activity from Myceliophthora thermophila. Process Biochem 61:110–118
doi: 10.1016/j.procbio.2017.06.017
Pala U, Yelmazer B, Çorbacıoglu M, Ruupunen J, Valjakka J, Turunen O, Binay B (2018) Functional effects of active site mutations in NAD+-dependent formate dehydrogenases on transformation of hydrogen carbonate to formate. Protein Eng Des Sel 31:327–335
doi: 10.1093/protein/gzy027
Lamzin VS, Dauter Z, Popov VO, Harutyunyan EH, Wilson KS (1994) High resolution structures of holo and apo formate dehydrogenase. JMolBiol 236:759–785
Guo Q, Gakhar L, Wickersham K, Francis K, Vardi-Kilshtain A, Major DT, Cheatum CM, Kohen A (2016) Structural and Kinetic Studies of Formate Dehydrogenase from. Candida boidiniiBiochemistry 55:2760–2771
Shabalin IG, Polyakov KM, Serov AE, Skirgello OE, Sadykhov EG, Dorovatovskiy PV, Tishkov VI, Popov VO (2010) NAD-dependent formate dehydrogenase from higher-plant Arabidopsis thaliana in complex with NAD and azide. PDB Databank
Filippova EV, Polyakov KM, Tikhonova TV, Sadykhov IG, Shabalin IG, Tishkov VI, Popov VO (2009) NAD-dependent formate dehydrogenase from bacterium Moraxella sp.C2 in complex with NAD and azide. Acta Crystallogr D Biol Crystallogr 65:1315–1325
doi: 10.1107/S0907444909040773
Yoch DC, Chen YP, Hardin MG (1990) Formate dehydrogenase from the methane oxidizer Methylosinus trichosporium OB3b. J Bacteriol 172:4456–4463
doi: 10.1128/JB.172.8.4456-4463.1990
Ding HT, Liu DF, Li ZL, Du YQ, Xu XH, Zhao YH (2011) Characterization of a thermally stable and organic solvent-adaptative NAD +-dependent formate dehydrogenase from Bacillus sp. F1. J Appl Microbiol 111:1075–1085
doi: 10.1111/j.1365-2672.2011.05124.x
Robinson WE, Bassegoda A, Reisner E, Hirst J (2017) Oxidation-State-Dependent Binding Properties of the Active Site in a Mo-Containing Formate Dehydrogenase. J Am Chem Soc 139:9927–9936
doi: 10.1021/jacs.7b03958
Schlapbach L, Züttel A (2010) Hydrogen-storage materials for mobile applications. in Materials for Sustainable Energy: A Collection of Peer-Reviewed Research and Review Articles from Nature Publishing Group 265–270
Srikanth S, Alvarez-Gallego Y, Vanbroekhoven K, Pant D (2017) Enzymatic Electrosynthesis of Formic Acid through Carbon Dioxide Reduction in a Bioelectrochemical System: Effect of Immobilization and Carbonic Anhydrase Addition. ChemPhysChem 18:3174–3181
doi: 10.1002/cphc.201700017
Liu A, Feng R, Liang B (2016) Microbial surface displaying formate dehydrogenase and its application in optical detection of formate. Enzyme Microb Technol 91:59–65
doi: 10.1016/j.enzmictec.2016.06.002
Yu S, Zhu L, Zhou C, An T, Zhang T, Jiang B, Mu W (2014) Promising properties of a formate dehydrogenase from a methanol- assimilating yeast Ogataea parapolymorpha DL-1 in His-tagged form. Appl Microbiol Biotechnol 98:1621–1630
doi: 10.1007/s00253-013-4996-5
Shannon RD (1976) Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides. Acta Crystallogr Sect A 32:751–767
doi: 10.1107/S0567739476001551
Shabalin IG, Filippova EV, Polyako KM, Sadykhov EG, Safonova TN, Tikhonova TV, Tishkov VI, Popov VO (2009) Structures of the apo and holo forms of formate dehydrogenase from the bacterium Moraxella sp. C-1: towards understanding the mechanism of the closure of the interdomain cleft. Acta Crystallogr SectD 65:1315–1325
Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH (2014) MMDB and VAST+: tracking structural similarities between macromolecular complexes. Nucleic Acids 42:297–303
doi: 10.1093/nar/gkt1208
Pagano P, Guo Q, Kohen A, and Christopher M (2016) Oscillatory Enzyme Dynamics Revealed by Two-Dimensional Infrared Spectroscopy. J Phys Chem Lett 7(13):2507–2511 7 )
doi: 10.1021/acs.jpclett.6b01154
Çakar MM, Mangas-Sanchez J, Birmingham WR, Turner NJ, Binay B (2018) Discovery of a new metal and NAD+-dependent formate dehydrogenase from Clostridium ljungdahlii. Prep Biochem Biotechnol 48:327–334
doi: 10.1080/10826068.2018.1446150
Karimäki J, Parkkinen T, Santa H, Pastinen O, Leisola M, Rouvinen J, Turunen O (2004) Engineering the substrate specificity of xylose isomerase. Protein Eng Des Sel 17:861–869
doi: 10.1093/protein/gzh099
Santa H, Kammonen J, Karimäki J, Leisola M, Turunen O (2005) Stochastic boundary molecular dynamics simulation of L-ribose in the active site of Actinoplanes missouriensis xylose isomerase and its Val135Asn mutant with improved reaction rate. Biochim Biophys Acta - Proteins Proteomics 1749:65–73
doi: 10.1016/j.bbapap.2005.02.007

Auteurs

Huri Bulut (H)

Medical Biochemistry Department, Faculty of Medicine, Istinye University, Istanbul, Turkey.

Jarkko Valjakka (J)

Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.

Busra Yuksel (B)

Molecular Biology and Genetics Department, Istanbul Technical University, Istanbul, Turkey.

Berin Yilmazer (B)

Molecular Biology and Genetics Department, Gebze Technical University, Kocaeli, Turkey.

Ossi Turunen (O)

School of Forest Sciences, Faculty of Science and Forestry, University of Eastern Finland, Joensuu, Finland.

Baris Binay (B)

Department of Bioengineering, Gebze Technical University, Kocaeli, Turkey. binay@gtu.edu.tr.

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Classifications MeSH