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1. Molecular mechanisms of oxygen activation
by Hayaishi, Osamu, 1920-2015
1974, Molecular biology; an international series of monographs and textbooks, 678
Oxygenases
Book
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2. Oxygenases
by Hayaishi, Osamu, 1920-2015
1962, 588
Oxygenases
Book
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3. Full Text Structure of a hyperthermostable dimeric archaeal Rubisco from Hyperthermus butylicus
by Bundela, Rudranuj and Keown, Jeremy and Watkin, Serena and Pearce, Frederick Grant
Acta Crystallographica Section D, ISSN 2059-7983, 06/2019, Volume 75, Issue 6, pp. 536 - 544
The crystal structure of ribulose‐1,5‐bisphosphate carboxylase/oxygenase (Rubisco) from the hyperthermophilic archaeon Hyperthermus butylicus is presented at... 
Rubisco | oligomerization | Hyperthermus butylicus | ribulose‐1,5‐bisphosphate carboxylase oxygenase | thermostability | Thermostability | Oligomerization | Ribulose-1,5-bisphosphate carboxylase oxygenase | MACROMOLECULES | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | 5-bisphosphate carboxylase oxygenase | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE RUBISCO | RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE | BIOCHEMICAL RESEARCH METHODS | CRYSTALLOGRAPHY | ribulose-1 | EVOLUTION | BIOPHYSICS | BISPHOSPHATE CARBOXYLASE/OXYGENASE | QUATERNARY STRUCTURE | PROTEINS | SCATTERING | Oxygenase | Enzymes | Denaturation | Ribulose-bisphosphate carboxylase | Thermal denaturation | Dimers | Electrostatic properties | Thermal stability | Crystal structure
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4. Heme oxygenase
: the elegant orchestration of its products in medicine
by Otterbein, Leo E and Zuckerbraun, Brian S
2005, ISBN 9781594544477, xiii, 417
Heme oxygenase
Book
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5. Full Text Publisher Correction: The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases
by Markolovic, Suzana and Zhuang, Qinqin and Wilkins, Sarah E and Eaton, Charlotte D and Abboud, Martine I and Katz, Maximiliano J and McNeil, Helen E and Leśniak, Robert K and Hall, Charlotte and Struwe, Weston B and Konietzny, Rebecca and Davis, Simon and Yang, Ming and Ge, Wei and Benesch, Justin L. P and Kessler, Benedikt M and Ratcliffe, Peter J and Cockman, Matthew E and Fischer, Roman and Wappner, Pablo and Chowdhury, Rasheduzzaman and Coleman, Mathew L and Schofield, Christopher J
Nature Chemical Biology, ISSN 1552-4450, 06/2018, Volume 14, Issue 10, pp. 1 - 988
In the version of this article initially published, authors Sarah E. Wilkins, Charlotte D. Eaton, Martine I. Abboud and Maximiliano J. Katz were incorrectly... 
Oxygenase | Hydroxylation
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6. Full Text Transcriptional and translational modulation of myo-inositol oxygenase (Miox) by fatty acids: Implications in renal tubular injury induced in obesity and diabetes
by Tominaga, Tatsuya and Dutta, Rajesh K and Joladarashi, Darukeshwara and Doi, Toshio and Reddy, Janardan K and Kanwar, Yashpal S
Journal of Biological Chemistry, ISSN 0021-9258, 01/2016, Volume 291, Issue 3, pp. 1348 - 1367
The kidney is one of the target organs for various metabolic diseases, including diabetes, metabolic syndrome, and obesity. Most of the metabolic studies... 
KIDNEY-DISEASE | METABOLIC SYNDROME | OXIDATIVE STRESS | PROTEIN | EPITHELIAL-CELLS | INSULIN-RESISTANCE | BIOCHEMISTRY & MOLECULAR BIOLOGY | OXIDOREDUCTASE/MYO-INOSITOL OXYGENASE | GENE-EXPRESSION | HIGH-GLUCOSE | ALBUMIN | Up-Regulation | Phosphorylation | Oxidative Stress | Diabetic Nephropathies - etiology | Humans | Diet, High-Fat - adverse effects | Male | Oxygenases - antagonists & inhibitors | RNA Interference | Inositol Oxygenase - metabolism | Oxygenases - metabolism | Obesity - etiology | Kidney Tubules - pathology | Kidney Tubules - metabolism | Sterol Regulatory Element Binding Protein 1 - metabolism | Cell Line | Promoter Regions, Genetic | Diabetic Nephropathies - pathology | Diabetic Nephropathies - metabolism | Rats | Obesity - metabolism | Obesity - pathology | Proteins - genetics | Animals | Proteins - metabolism | Inositol Oxygenase - antagonists & inhibitors | Sterol Regulatory Element Binding Protein 1 - genetics | Kidney Tubules - enzymology | Sterol Regulatory Element Binding Protein 1 - antagonists & inhibitors | Inositol Oxygenase - genetics | Mice | Protein Processing, Post-Translational | Oxygenases - genetics | Proteins - antagonists & inhibitors | Sus scrofa | Apoptosis | Index Medicus | kidney | renal tubular injury | kidney metabolism | fatty acid | myo-inositol oxygenase | Metabolism | diabetic nephropathy | obesity
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7. Heme oxygenase
: clinical applications and functions
by Maines, Mahin D
1992, ISBN 9780849354083, 276
Jaundice, Neonatal | Pathophysiology | Metabolism | Heme oxygenase | Heme
Book
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8. Full Text Inactivation of the heme degrading enzyme IsdI by an active site substitution that diminishes heme ruffling
by Ukpabi, Georgia and Takayama, Shin-Ichi J and Mauk, A. Grant and Murphy, Michael E. P
Journal of Biological Chemistry, ISSN 0021-9258, 10/2012, Volume 287, Issue 41, pp. 34179 - 34188
IsdG and IsdI are paralogous heme degrading enzymes from the bacterium Staphylococcus aureus. Heme bound by these enzymes is extensively ruffled such that the... 
HYDROXIDE COMPLEX | CORYNEBACTERIUM-DIPHTHERIAE | ELECTRONIC-STRUCTURES | BIOCHEMISTRY & MOLECULAR BIOLOGY | CYTOCHROMES-B | PORPHYRINS | STRUCTURAL-CHARACTERIZATION | STAPHYLOCOCCUS-AUREUS | OXYGENASE | CATALYTIC SITE | PSEUDOMONAS-AERUGINOSA HEME | Heme - metabolism | Oxidation-Reduction | Humans | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Oxygenases - chemistry | Mutation, Missense | Staphylococcus aureus - chemistry | Heme - chemistry | Heme - genetics | Oxygenases - metabolism | Nuclear Magnetic Resonance, Biomolecular | Bacterial Proteins - metabolism | Catalysis | Oxygenases - genetics | Mixed Function Oxygenases - genetics | Staphylococcus aureus - drug effects | Amino Acid Substitution | Index Medicus | Site-directed Mutagenesis | X-ray Crystallography | Enzyme Catalysis | Heme | Electrochemistry | Heme Oxygenase | Enzymology
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9. Oxygenases
by Hayaishi, O
1962, xii, 588
oxygenases
Book
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10. Oxygenases
by Hayaishi, Osamu, 1920- ed
1962, xii, 588 p. illus., diagrs.
Oxygenases
Book
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11. Full Text IsdG and IsdI, Heme-degrading Enzymes in the Cytoplasm of Staphylococcus aureus
by Eric P. Skaar and Andrew H. Gaspar and Olaf Schneewind
Journal of Biological Chemistry, ISSN 0021-9258, 01/2004, Volume 279, Issue 1, pp. 436 - 443
Staphylococcus aureus requires iron for growth and utilizes heme as a source of iron during infection. Staphylococcal surface proteins capture hemoglobin,... 
HEMOGLOBIN | CORYNEBACTERIUM-DIPHTHERIAE | OUTER-MEMBRANE | GRAM-NEGATIVE BACTERIA | SURFACE PROTEIN | PORPHYROMONAS-GINGIVALIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | IRON | IDENTIFICATION | OXYGENASE HMU O | COUPLED OXIDATION | Biodegradation, Environmental | Consensus Sequence | Oxygenases - isolation & purification | Recombinant Proteins - metabolism | Staphylococcus aureus - genetics | Cytoplasm - enzymology | Staphylococcus aureus - enzymology | Escherichia coli - enzymology | DNA Primers | Iron - metabolism | Heme Oxygenase (Decyclizing) - isolation & purification | Recombinant Proteins - isolation & purification | Escherichia coli - genetics | Oxygenases - metabolism | Base Sequence | Heme - pharmacokinetics | Cloning, Molecular | Polymerase Chain Reaction | Kinetics | Oxygenases - genetics | Heme Oxygenase (Decyclizing) - metabolism | Heme Oxygenase (Decyclizing) - genetics | Index Medicus
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12. Full Text The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure
by Yachnin, Brahm J and Lau, Peter C.K and Berghuis, Albert M
BBA - Proteins and Proteomics, ISSN 1570-9639, 12/2016, Volume 1864, Issue 12, pp. 1641 - 1648
The Baeyer-Villiger monooxygenases (BMVOs) are a group of microbial enzymes that have garnered interest as industrial biocatalysts. While great strides have... 
Isothermal titration calorimetry (ITC) | Baeyer-Villiger monooxygenase | Enzyme mechanism | Enzyme catalysis | Small-angle X-ray scattering (SAXS) | Protein flexibility | ACINETOBACTER NCIB-9871 | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-SCATTERING | CYCLOHEXANONE MONOOXYGENASE | BIOPHYSICS | OXYGENASE | PROTEINS | Bacterial Proteins - chemistry | Crystallography, X-Ray | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Acinetobacter - enzymology | Oxygenases - metabolism | X-Ray Diffraction | NADP - metabolism | Rhodococcus - enzymology | Biocatalysis | Mutagenesis, Site-Directed | Bacterial Proteins - genetics | Catalytic Domain - genetics | Enzyme Stability | Models, Molecular | Scattering, Small Angle | Acinetobacter - genetics | Oxygenases - chemistry | Rhodococcus - genetics | Bacterial Proteins - metabolism | Calorimetry | Protein Conformation | Kinetics | Oxygenases - genetics | Mixed Function Oxygenases - genetics | Enzymes | Catalysis | Analysis
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13. Full Text Genetic dissection in a mouse model reveals interactions between carotenoids and lipid metabolism
by Palczewski, Grzegorz and Widjaja-Adhi, M. Airanthi K and Amengual, Jaume and Golczak, Marcin and Von Lintig, Johannes
Journal of Lipid Research, ISSN 0022-2275, 09/2016, Volume 57, Issue 9, pp. 1684 - 1695
Carotenoids affect a rich variety of physiological functions in nature and are beneficial for human health. However, knowledge about their biological action... 
Zeaxanthin | β-carotene-9 | Lipoproteins | β-carotene-15 | Liver | 10′-oxygenase | β-carotene | 15′-oxygenase | Microarray | Triglyceride | Cholesterol | triglyceride | beta,beta-carotene-15,15 '-oxygenase | liver | beta-carotene | BIOCHEMISTRY & MOLECULAR BIOLOGY | beta,beta-carotene-9 ',10 '-oxygenase | VITAMIN-A PRODUCTION | IDENTIFICATION | zeaxanthin | microarray | COLOR | MUTATION | DISEASE | cholesterol | LUTEIN | 15,15-MONOOXYGENASE | OXIDATIVE CLEAVAGE | lipoproteins | ADIPOSE-TISSUE | beta Carotene - blood | Lipids - genetics | Cholesterol - blood | Humans | Liver - metabolism | Lipid Metabolism | Transcriptome - genetics | beta Carotene - administration & dosage | Cholesterol - genetics | Lutein - blood | Lipolysis - genetics | Animals | Diet | Liver - drug effects | Lutein - administration & dosage | Lipids - blood | Carotenoids - metabolism | Triglycerides - blood | Zeaxanthins - administration & dosage | Mice | Triglycerides - genetics | Energy Metabolism - genetics | Metabolism - genetics | Disease Models, Animal | Index Medicus | β,β-carotene-15,15′-oxygenase | β,β-carotene-9′,10′-oxygenase
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14. Full Text The IsdG-family of haem oxygenases degrades haem to a novel chromophore
by Reniere, Michelle L and Ukpabi, Georgia N and Harry, S. Reese and Stec, Donald F and Krull, Robert and Wright, David W and Bachmann, Brian O and Murphy, Michael E and Skaar, Eric P
Molecular Microbiology, ISSN 0950-382X, 2010, Volume 75, Issue 6, pp. 1529 - 1538
P>Enzymatic haem catabolism by haem oxygenases is conserved from bacteria to humans and proceeds through a common mechanism leading to the formation of iron,... 
CORYNEBACTERIUM-DIPHTHERIAE | GRAM-NEGATIVE BACTERIA | MECHANISM | CRYSTAL-STRUCTURE | PSEUDOMONAS-AERUGINOSA | ENZYMES | PRODUCT | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEGRADATION | MICROBIOLOGY | STAPHYLOCOCCUS-AUREUS | IRON | Protein Structure, Tertiary | Staphylococcus aureus - enzymology | Heme - metabolism | Oxidation-Reduction | Bacterial Proteins - chemistry | Models, Molecular | Crystallography, X-Ray | Mixed Function Oxygenases - metabolism | Mixed Function Oxygenases - chemistry | Oxygenases - chemistry | Heme Oxygenase (Decyclizing) - chemistry | Oxygenases - metabolism | Bacterial Proteins - metabolism | Molecular Structure | Heme Oxygenase (Decyclizing) - metabolism | Oxidases | Carbon monoxide | Structure | Crystals | Heme | Enzymes | Staphylococcus infections | Iron | Microbiology | Metabolism | Index Medicus
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15. Full Text Unexpected roles for ancient proteins: flavone 8‐hydroxylase in sweet basil trichomes is a Rieske‐type, PAO‐family oxygenase
by Berim, Anna and Park, Jeong‐Jin and Gang, David R
The Plant Journal, ISSN 0960-7412, 11/2014, Volume 80, Issue 3, pp. 385 - 395
Most elucidated hydroxylations in plant secondary metabolism are catalyzed by oxoglutarate‐ or cytochrome P450‐dependent oxygenases. Numerous hydroxylations... 
ieske‐type oxygenase | specialized metabolism | methoxylated flavonoids | cimum basilicum | hydroxylase | PTC | Specialized metabolism | Methoxylated flavonoids | PTC52 | Rieske-type oxygenase | Hydroxylase | Ocimum basilicum | ARABIDOPSIS-THALIANA | CHOLINE MONOOXYGENASE | PLANT EVOLUTION | PLANT SCIENCES | GENE | POLYPHENOL OXIDASE | CLONING | FUNCTIONAL EXPRESSION | BIOSYNTHESIS | NONHEME OXYGENASES | DIVERSITY | Amino Acid Sequence | Flavones - metabolism | Molecular Sequence Data | Mixed Function Oxygenases - metabolism | Trichomes - enzymology | Flavones - chemistry | Phylogeny | Recombinant Proteins | Sequence Analysis, DNA | Sequence Homology, Amino Acid | Plant Proteins - genetics | Ocimum basilicum - enzymology | Plant Leaves - genetics | Oxygenases - metabolism | Base Sequence | Ocimum basilicum - genetics | Trichomes - genetics | Plant Proteins - metabolism | Oxygenases - genetics | Mixed Function Oxygenases - genetics | Plant Leaves - enzymology | Oxidases | Peptides | Genomics | Plant genetics | Physiological aspects | Plants | Isoflavones | Proteins | Plant biology | Enzymes | Metabolism | Genes | Index Medicus
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16. Full Text Crystal structure of CmlI, the arylamine oxygenase from the chloramphenicol biosynthetic pathway
by Knoot, Cory J and Kovaleva, Elena G and Lipscomb, John D and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
JBIC Journal of Biological Inorganic Chemistry, ISSN 0949-8257, 9/2016, Volume 21, Issue 5, pp. 589 - 603
The diiron cluster-containing oxygenase CmlI catalyzes the conversion of the aromatic amine precursor of chloramphenicol to the nitroaromatic moiety of the... 
Life Sciences | Biochemistry, general | Oxygen activation | Microbiology | Peroxo intermediate | Arylamine oxygenase | Antibiotic biosynthesis | Non-heme iron | Diiron cluster | ACTIVE-SITE | DEOXYHYPUSINE HYDROXYLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PEROXODIFERRIC INTERMEDIATE | CHEMISTRY, INORGANIC & NUCLEAR | ACYL CARRIER PROTEIN | METHANE MONOOXYGENASE HYDROXYLASE | RIBONUCLEOTIDE REDUCTASE | N-OXYGENASE | STREPTOMYCES-VENEZUELAE ISP5230 | COMPONENT-B | Chloramphenicol - chemistry | Oxygenases - metabolism | Molecular Conformation | Chloramphenicol - biosynthesis | Models, Molecular | Crystallography, X-Ray | Oxygenases - chemistry | Oxygenases - genetics | Oxidases | Analysis | Heme | Crystals | Physiological aspects | Chloramphenicol | Structure | Oxygenase | Iron | pH effects | Crystal structure | Index Medicus
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17. Full Text An endogenous tumour-promoting ligand of the human aryl hydrocarbon receptor
by Opitz, Christiane A and Litzenburger, Ulrike M and Sahm, Felix and Ott, Martina and Tritschler, Isabel and Trump, Saskia and Schumacher, Theresa and Jestaedt, Leonie and Schrenk, Dieter and Weller, Michael and Jugold, Manfred and Guillemin, Gilles J and Miller, Christine L and Lutz, Christian and Radlwimmer, Bernhard and Lehmann, Irina and Von Deimling, Andreas and Wick, Wolfgang and Platten, Michael
Nature, ISSN 0028-0836, 10/2011, Volume 478, Issue 7368, pp. 197 - 203
Activation of the aryl hydrocarbon receptor (AHR) by environmental xenobiotic toxic chemicals, for instance 2,3,7,8-tetrachlorodibenzo-p-dioxin (dioxin), has... 
KYNURENINE | INHIBITION | INFLAMMATION | MULTIDISCIPLINARY SCIENCES | INDOLEAMINE 2,3-DIOXYGENASE | REGULATORY T-CELLS | AH RECEPTOR | TRYPTOPHAN 2,3-DIOXYGENASE | MICE | DIFFERENTIATION | CANCER | Neoplasm Transplantation | Humans | Brain Neoplasms - pathology | Gene Expression Regulation, Neoplastic | Tryptophan - metabolism | Brain Neoplasms - metabolism | Glioma - metabolism | Glioma - genetics | Brain Neoplasms - immunology | Glioma - pathology | Receptors, Aryl Hydrocarbon - metabolism | Kynurenine - metabolism | Autocrine Communication | Paracrine Communication | Cell Survival | Kynurenine - pharmacology | Mice, Inbred C57BL | Brain Neoplasms - genetics | Glioma - immunology | Disease Progression | Tryptophan Oxygenase - metabolism | Tryptophan Oxygenase - genetics | Animals | Mice, Nude | Kynurenine - secretion | Cell Line, Tumor | Ligands | Mice | Tryptophan Oxygenase - deficiency | Kynurenine - immunology | Receptors, Aryl Hydrocarbon - immunology | Index Medicus
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18. Full Text Evidence of Arabidopsis salt acclimation induced by up‐regulation of HY1 and the regulatory role of RbohD‐derived reactive oxygen species synthesis
by Xie, Yan‐Jie and Xu, Sheng and Han, Bin and Wu, Ming‐Zhu and Yuan, Xing‐Xing and Han, Yi and Gu, Quan and Xu, Dao‐Kun and Yang, Qing and Shen, Wen‐Biao
The Plant Journal, ISSN 0960-7412, 04/2011, Volume 66, Issue 2, pp. 280 - 292
In Arabidopsis thaliana , a family of four genes ( HY1 , HO2 , HO3 and HO4 ) encode haem oxygenase (HO), and play a major role in phytochrome chromophore... 
HY1 | salt acclimation | RbohD | Arabidopsis | reactive oxygen species | NADPH OXIDASE | OXIDATIVE STRESS | SEED-GERMINATION | PHYTOCHROME CHROMOPHORE BIOSYNTHESIS | NACL PRETREATMENT | OXYGENASE/CARBON MONOXIDE SYSTEM | HEME-OXYGENASE | CELL-DEATH | PLANT SCIENCES | CARBON-MONOXIDE | HYDROGEN-PEROXIDE | Arabidopsis Proteins - genetics | Arabidopsis - enzymology | Reactive Oxygen Species - metabolism | Plants, Genetically Modified - genetics | NADPH Oxidases - metabolism | Plants, Genetically Modified - enzymology | Plant Roots - genetics | Acclimatization | Salinity | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Gene Expression Regulation, Plant | Plant Roots - enzymology | NADPH Oxidases - genetics | Salt-Tolerant Plants - enzymology | Mutagenesis, Insertional | Heme Oxygenase (Decyclizing) - metabolism | Heme Oxygenase (Decyclizing) - genetics | Salt-Tolerant Plants - genetics | Arabidopsis thaliana | Physiological aspects | Chromophores | Superoxide | Phytochrome | Plant biology | Salt | Enzymes | Flowers & plants | Abiotic stress | Index Medicus
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