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biochemistry & molecular biology (73) 73
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International Journal of Biological Macromolecules, ISSN 0141-8130, 04/2019, Volume 127, pp. 585 - 593
Journal Article
Journal Article
DALTON TRANSACTIONS, ISSN 1477-9226, 05/2019, Volume 48, Issue 18, pp. 6083 - 6090
The crystal structure of Bacillus subtilis SirB, which catalyses the insertion of Fe2+ into the substrate sirohydrochlorin (SHC) in siroheme biosynthesis, is... 
INSERTION | METAL-ION | PROTEIN | BACILLUS-SUBTILIS FERROCHELATASE | CRYSTAL-STRUCTURE | COBALTOCHELATASE | SIROHEME BIOSYNTHESIS | COBALAMIN | IDENTIFICATION | TERMINAL ENZYME | CHEMISTRY, INORGANIC & NUCLEAR
Journal Article
Journal Article
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, ISSN 0003-9861, 04/2018, Volume 644, pp. 37 - 46
Journal Article
JBIC Journal of Biological Inorganic Chemistry, ISSN 0949-8257, 2/2011, Volume 16, Issue 2, pp. 235 - 242
Journal Article
PLoS ONE, ISSN 1932-6203, 02/2013, Volume 8, Issue 2, p. e55569
Heme is a cofactor for proteins participating in many important cellular processes, including respiration, oxygen metabolism and oxygen binding. The key enzyme... 
ARABIDOPSIS-THALIANA | CAB-LIKE-PROTEINS | BACILLUS-SUBTILIS FERROCHELATASE | HEME-BIOSYNTHESIS | HIGHER-PLANTS | MULTIDISCIPLINARY SCIENCES | PHOTOSYSTEM-II | SUBCELLULAR-LOCALIZATION | SP PCC-6803 | TETRAPYRROLE BIOSYNTHESIS | CHLOROPHYLL SYNTHESIS | Heme - metabolism | Light-Harvesting Protein Complexes - genetics | Inclusion Bodies - chemistry | Bacterial Proteins - chemistry | Light-Harvesting Protein Complexes - metabolism | Molecular Sequence Data | Chlorophyll Binding Proteins - metabolism | Pigments, Biological - metabolism | Coenzymes - metabolism | Heme - chemistry | Synechocystis - enzymology | Plastids - genetics | Ferrochelatase - chemistry | Synechocystis - genetics | Coenzymes - chemistry | Light-Harvesting Protein Complexes - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Catalytic Domain | Bacterial Proteins - genetics | Protein Refolding | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Amino Acid Motifs | Sequence Homology, Amino Acid | Plastids - enzymology | Chlorophyll Binding Proteins - genetics | Escherichia coli - genetics | Ferrochelatase - metabolism | Bacterial Proteins - metabolism | Ferrochelatase - genetics | Chlorophyll Binding Proteins - chemistry | Kinetics | Pigments, Biological - chemistry | Physiological aspects | Genetic aspects | Research | Photosynthesis | Enzyme kinetics | Cyanobacteria | Membranes | Homology | Iron and steel plants | Biosynthesis | Iron | Genomes | Biochemistry | Hydrophobicity | Proteins | Mitochondria | Protoporphyrin | Chloroplasts | Light | Inclusion bodies | Heme | Reaction kinetics | Pigments | Magnesium | Plant sciences | Localization | Recombinant | Binding | Chlorophyll | Plants (botany) | Oxygen | Oxygen metabolism | Ferrochelatase | Gene expression | Metabolism | Protoporphyrin IX | Enzymology | Biological Sciences | Naturvetenskap | biokemi | Biokemi och molekylärbiologi | Biologiska vetenskaper | Biochemistry and Molecular Biology | Natural Sciences
Journal Article
Journal of Porphyrins and Phthalocyanines, ISSN 1088-4246, 04/2016, Volume 20, Issue 1-4, pp. 556 - 569
Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX to generate heme. Despite recent research on the reaction mechanism of... 
enzyme | tetrapyrrole | molecular dynamic simulations | porphyrin | protoporphyrin IX | p K a | PropKa | iron | porphyrin metalation | chelatase | CHARMM | ferrochelatase | WILD-TYPE | DIRECTED MUTAGENESIS | ION | CHEMISTRY, MULTIDISCIPLINARY | BACILLUS-SUBTILIS FERROCHELATASE | PROTOPORPHYRIN-IX | pK(a) | BINDING-SITE | IRON-BINDING | MAMMALIAN FERROCHELATASE | RESIDUES | PRODUCT RELEASE
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2010, Volume 285, Issue 53, pp. 41836 - 41841
Journal Article
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2009, Volume 284, Issue 49, pp. 33795 - 33799
Protoporphyrin IX ferrochelatase (EC 4.99.1.1) catalyzes the terminal step in the heme biosynthetic pathway, the insertion of ferrous iron into protoporphyrin... 
ZINC PROTOPORPHYRIN | SPECIFICITY CONSTANTS | HEME-BIOSYNTHESIS | N-METHYLPROTOPORPHYRIN | BACILLUS-SUBTILIS | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | 2-SUBSTRATE ENZYMES | TERMINAL ENZYME | BINDING | PRODUCT RELEASE | Models, Chemical | Detergents - chemistry | Humans |