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molybdoferredoxin - metabolism (283) 283
science & technology (261) 261
nitrogenase - metabolism (251) 251
molybdoferredoxin - chemistry (187) 187
life sciences & biomedicine (182) 182
biochemistry & molecular biology (153) 153
nitrogenase - chemistry (149) 149
nitrogenase (133) 133
oxidation-reduction (118) 118
models, molecular (95) 95
electron spin resonance spectroscopy (93) 93
azotobacter vinelandii - enzymology (89) 89
chemistry (84) 84
kinetics (82) 82
biological and medical sciences (81) 81
fundamental and applied biological sciences. psychology (78) 78
physical sciences (78) 78
binding sites (73) 73
protein conformation (68) 68
molybdoferredoxin - genetics (67) 67
research (61) 61
nitrogenase - genetics (60) 60
adenosine triphosphate - metabolism (59) 59
nitrogen fixation (59) 59
oxidoreductases (58) 58
bacterial proteins - metabolism (55) 55
molybdenum (55) 55
proteins (54) 54
klebsiella pneumoniae - enzymology (53) 53
electron transport (51) 51
analysis (50) 50
catalysis (50) 50
azotobacter vinelandii - metabolism (47) 47
biochemistry (46) 46
ferredoxins - metabolism (45) 45
chemical properties (40) 40
mutation (39) 39
research article (38) 38
chemistry, multidisciplinary (37) 37
amino acid sequence (36) 36
azotobacter vinelandii - genetics (36) 36
microbiology (36) 36
molecular sequence data (36) 36
molybdoferredoxin - biosynthesis (36) 36
nitrogen (36) 36
iron (35) 35
molybdenum - metabolism (35) 35
protein binding (35) 35
analytical, structural and metabolic biochemistry (34) 34
azotobacter - enzymology (34) 34
molybdoferredoxin - isolation & purification (33) 33
substrate specificity (33) 33
genes, bacterial (32) 32
bacterial proteins - chemistry (31) 31
chemistry, inorganic & nuclear (31) 31
enzymes (31) 31
multidisciplinary sciences (31) 31
science & technology - other topics (31) 31
nitrogen - metabolism (30) 30
crystallography, x-ray (29) 29
electrons (29) 29
azotobacter vinelandii (28) 28
bacterial proteins - genetics (28) 28
enzymes and enzyme inhibitors (28) 28
hydrogen - metabolism (28) 28
molecular structure (28) 28
mutagenesis, site-directed (28) 28
klebsiella pneumoniae - genetics (27) 27
hydrolysis (25) 25
ligands (25) 25
models, chemical (25) 25
bacteriology (24) 24
catalytic domain (24) 24
iron - metabolism (24) 24
nitrogen - chemistry (24) 24
iron - chemistry (23) 23
mofe protein (22) 22
molybdenum - chemistry (21) 21
spectrum analysis (21) 21
acetylene - metabolism (20) 20
macromolecular substances (20) 20
metalloproteins (20) 20
nitrogen fixation - genetics (20) 20
physiological aspects (20) 20
azotobacter vinelandii - chemistry (19) 19
bacteria (19) 19
humans (19) 19
biological sciences (18) 18
metabolism. enzymes (18) 18
protons (18) 18
structure (18) 18
ammonia (17) 17
biophysics (17) 17
biosynthesis (17) 17
klebsiella pneumoniae - metabolism (17) 17
molybdoferredoxin (17) 17
nitrogenase - isolation & purification (17) 17
oxidation-reduction reaction (17) 17
usage (17) 17
oxidoreductases - metabolism (16) 16
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1. Full Text Emerging Paradigms for Complex Iron-Sulfur Cofactor Assembly and Insertion
by Peters, John W and Broderick, Joan B
Annual review of biochemistry, ISSN 0066-4154, 7/2012, Volume 81, Issue 1, pp. 429 - 450
hydrogenase | biogenesis | radical SAM | H cluster | nitrogenase | FeMo cofactor | Sulfur - metabolism | Bacteria - metabolism | Molybdoferredoxin - metabolism | Branchial Region - metabolism | Hydrogenase - chemistry | Iron-Sulfur Proteins - chemistry | Branchial Region - enzymology | Iron - metabolism | Coenzymes - metabolism | Hydrogenase - metabolism | Molybdoferredoxin - chemistry | Bacteria - enzymology | Iron-Sulfur Proteins - metabolism | Coenzymes - chemistry | S-Adenosylmethionine - metabolism | Physiological aspects | Iron in the body | Properties | Nitrogenase | Enzymes | Biochemistry | Catalysis | Molecular structure | Chemical synthesis | Chemical compounds | Index Medicus
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2. Full Text Radical AdoMet enzymes in complex metal cluster biosynthesis
by Duffus, Benjamin R and Hamilton, Trinity L and Shepard, Eric M and Boyd, Eric S and Peters, John W and Broderick, Joan B
Biochimica et biophysica acta. Proteins and proteomics, ISSN 1570-9639, 11/2012, Volume 1824, Issue 11, pp. 1254 - 1263
Radical S-adenosylmethionine enzyme | Hydrogenase | Biosynthesis | Scaffold protein | Nitrogenase | Iron–sulfur cluster | Iron-sulfur cluster | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Sulfur - metabolism | Biocatalysis | Molybdoferredoxin - metabolism | Nitrogenase - metabolism | Free Radicals - chemistry | Iron - chemistry | Nitrogenase - chemistry | Bacterial Proteins - chemistry | Models, Molecular | Coordination Complexes - metabolism | S-Adenosylmethionine - chemistry | Hydrogenase - chemistry | Iron-Sulfur Proteins - chemistry | Phylogeny | Coordination Complexes - chemistry | Iron - metabolism | Hydrogenase - metabolism | Free Radicals - metabolism | Molybdoferredoxin - chemistry | Bacterial Proteins - metabolism | Iron-Sulfur Proteins - metabolism | S-Adenosylmethionine - metabolism | Evolution, Molecular | Sulfur - chemistry | Sulfur compounds | Enzymes | Chromatin | Iron compounds | Physiological aspects | S-adenosylmethionine
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3. Full Text Evidence That the Pi Release Event Is the Rate-Limiting Step in the Nitrogenase Catalytic Cycle
by Yang, Zhi-Yong and Ledbetter, Rhesa and Shaw, Sudipta and Pence, Natasha and Tokmina-Lukaszewska, Monika and Eilers, Brian and Guo, Qingjuan and Pokhrel, Nilisha and Cash, Valerie L and Dean, Dennis R and Antony, Edwin and Bothner, Brian and Peters, John W and Seefeldt, Lance C and Energy Frontier Research Centers (EFRC) (United States). Center for Biological Electron Transfer and Catalysis (BETCy)
Biochemistry (Easton), ISSN 0006-2960, 07/2016, Volume 55, Issue 26, pp. 3625 - 3635
Hydrolysis | Electron Transport | Molybdoferredoxin - metabolism | Nitrogenase - metabolism | Oxidation-Reduction | Oxidoreductases - metabolism | Adenosine Triphosphate - metabolism | Nitrogenase - chemistry | Molybdoferredoxin - chemistry | Protein Conformation | Catalysis | Azotobacter vinelandii - metabolism | Index Medicus | BASIC BIOLOGICAL SCIENCES | biofuels (including algae and biomass) | solar (fuels) | hydrogen and fuel cells | bio-inspired
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4. Full Text So Close, yet Sulfur Away: Opening the Nitrogenase Cofactor Structure Creates a Binding Site
by Skubi, Kazimer L and Holland, Patrick L
Biochemistry (Easton), ISSN 0006-2960, 07/2018, Volume 57, Issue 26, pp. 3540 - 3541
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Sulfur - metabolism | Bacteria - metabolism | Nitrogen - metabolism | Bacteria - chemistry | Molybdoferredoxin - metabolism | Nitrogenase - metabolism | Nitrogenase - chemistry | Bacterial Proteins - chemistry | Models, Molecular | Substrate Specificity | Nitrogen - chemistry | Molybdoferredoxin - chemistry | Bacteria - enzymology | Bacterial Proteins - metabolism | Protein Conformation | Binding Sites | Sulfur - chemistry | Index Medicus
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5. Full Text Molybdenum cofactor deficiency: Mutations in GPHN, MOCS1, and MOCS2
by Reiss, Jochen and Hahnewald, Rita
Human mutation, ISSN 1059-7794, 01/2011, Volume 32, Issue 1, pp. 10 - 18
MOCS2 | MoCo | MOCS3 | molybdenum cofactor | MOCS1 | GPHN | Molybdenum cofactor | Life Sciences & Biomedicine | Genetics & Heredity | Science & Technology | Metal Metabolism, Inborn Errors - genetics | Molybdoferredoxin - genetics | Membrane Proteins - genetics | Alternative Splicing - genetics | Humans | Metal Metabolism, Inborn Errors - pathology | Sulfurtransferases - genetics | Therapies, Investigational | Nuclear Proteins - metabolism | Carrier Proteins - genetics | Phenotype | Animals | Carrier Proteins - metabolism | Metal Metabolism, Inborn Errors - diagnosis | Membrane Proteins - metabolism | Mutation | Nuclear Proteins - genetics | Sulfurtransferases - metabolism | Disease Models, Animal | Index Medicus
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6. Full Text Urinary AASA excretion is elevated in patients with molybdenum cofactor deficiency and isolated sulphite oxidase deficiency
by Mills, P.B and Footitt, E.J and Ceyhan, S and Waters, P.J and Jakobs, C.A.J.M and Clayton, P.T and Struijs, E.A
Journal of inherited metabolic disease, ISSN 0141-8955, 2012, Volume 35, Issue 6, pp. 1031 - 1036
Biochemistry, general | Human Genetics | Pediatrics | Internal Medicine | Medicine & Public Health | Metabolic Diseases | Endocrinology & Metabolism | Genetics & Heredity | Life Sciences & Biomedicine | Medicine, Research & Experimental | Science & Technology | Research & Experimental Medicine | Biological and medical sciences | Metabolic diseases | Medical sciences | Medical genetics | Cysteine - analogs & derivatives | Metal Metabolism, Inborn Errors - metabolism | Humans | Pteridines | Sulfite Oxidase - deficiency | Sulfites - pharmacology | Amino Acid Metabolism, Inborn Errors - metabolism | Amino Acid Metabolism, Inborn Errors - urine | Cysteine - pharmacology | Coenzymes - deficiency | Metalloproteins - deficiency | Oxidoreductases Acting on Sulfur Group Donors - deficiency | Lysine - metabolism | Sulfite Oxidase - urine | 2-Aminoadipic Acid - analogs & derivatives | Child | Infant, Newborn | Molybdoferredoxin - urine | 2-Aminoadipic Acid - urine | Molybdoferredoxin - metabolism | L-Aminoadipate-Semialdehyde Dehydrogenase - antagonists & inhibitors | Metabolic Networks and Pathways | Models, Biological | Metal Metabolism, Inborn Errors - urine | Adolescent | Sulfite Oxidase - metabolism | Oxidases | Sulfites | Care and treatment | Molecular genetics | Analysis | Children's hospitals | Epilepsy | Molybdenum | Index Medicus
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7. Full Text Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor
by Spatzal, Thomas and Perez, Kathryn A and Howard, James B and Rees, Douglas C
eLife, ISSN 2050-084X, 12/2015, Volume 4, Issue 2015, pp. e11620 - e11620
Biology | Life Sciences & Biomedicine - Other Topics | Life Sciences & Biomedicine | Science & Technology | Catalytic Domain | Molybdoferredoxin - metabolism | Selenium - metabolism | Nitrogenase - metabolism | Models, Molecular | Molybdoferredoxin - chemistry | Crystallography, X-Ray | Cyanates - metabolism | Protein Conformation | Selenium Compounds - metabolism | Azotobacter vinelandii - chemistry | Azotobacter vinelandii - enzymology | Chemical reactions | Selenium | Chemical properties | Copper | Observations | Index Medicus
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8. Full Text The NifZ accessory protein has an equivalent function in maturation of both nitrogenase MoFe protein P-clusters
by Jimenez-Vicente, Emilio and Yang, Zhi-Yong and del Campo, Julia S. Martin and Cash, Valerie L and Seefeldt, Lance C and Dean, Dennis R
The Journal of biological chemistry, ISSN 0021-9258, 04/2019, Volume 294, Issue 16, pp. 6204 - 6213
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Molybdoferredoxin - genetics | Molybdoferredoxin - metabolism | Nitrogenase - metabolism | Bacterial Proteins - genetics | Bacterial Proteins - metabolism | Nitrogenase - genetics | Azotobacter vinelandii - metabolism | Azotobacter vinelandii - genetics | Index Medicus | Editors' Picks | maturation | nitrogen metabolism | FeMo-cofactor | iron-sulfur protein | NifW | NifZ | nitrogen fixation | Azotobacter vinelandii | metalloenzyme | nitrogenase | P-cluster
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9. Full Text Catalytic conversion of nitrogen to ammonia by an iron model complex
by Anderson, John S and Rittle, Jonathan and Peters, Jonas C
Nature (London), ISSN 0028-0836, 2013, Volume 501, Issue 7465, pp. 84 - 87
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Chemistry | General and physical chemistry | Catalysis | Theory of reactions, general kinetics. Catalysis. Nomenclature, chemical documentation, computer chemistry | Exact sciences and technology | Molybdenum - chemistry | Molybdoferredoxin - metabolism | Nitrogenase - metabolism | Oxidation-Reduction | Molybdenum - metabolism | Iron - chemistry | Nitrogenase - chemistry | Boranes - chemistry | Phosphines - chemistry | Biomimetics | Nitrogen - chemistry | Ammonia - chemical synthesis | Molybdoferredoxin - chemistry | Ammonia - chemistry | Nitrogen Fixation | Ammonia | Oxidation-reduction reaction | Iron | Research | Properties | Enzymes | Temperature | Ligands | Software | Nitrogen | Molybdenum | Binding sites | Index Medicus
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