Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 554

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Metalloenzymes, Structural Motifs, and Inorganic Models

Karlin, Kenneth D.·1993·Science
DOI 10.1126/science.7688141
Open this paper in CoChat — free account

Abstract

Metalloenzymes effect a variety of important chemical transformations, often involving small molecule substrates or products such as molecular oxygen, hydrogen, nitrogen, and water. A diverse array of ions or metal clusters is observed at the active-site cores, but living systems use basic recurring structures that have been modified or tuned for specific purposes. Inorganic chemists are actively involved in the elucidation of the structure, spectroscopy, and mechanism of action of these biological catalysts, in part through a synthetic modeling approach involving biomimetic studies.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1126/science.7688141

Cites

4 of 4 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 167

  1. JOURNAL OF BIOENERGETICS AND BIOMEMBRANES 25 2 (1993).
  2. ARMSTRONG, W.H., (MU-OXO)BIS(MU-ACETATO)BIS(TRI-1-PYRAZOLYLBORATO)DIIRON-(III), [(HBPZ3)FEO(CH3CO2)2FE(HBPZ3)] - MODEL FOR THE BINUCLEAR IRON CENTER OF HEMERYTHRIN, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 105: 4837 (1983). · DOI
  3. Armstrong, W. H., Metal Clusters in Proteins: 1 (1988).
  4. ATTA, M, SUBSTITUTION OF MANGANESE FOR IRON IN RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA-COLI - SPECTROSCOPIC AND CRYSTALLOGRAPHIC CHARACTERIZATION, JOURNAL OF BIOLOGICAL CHEMISTRY 267: 20682 (1992). · DOI
  5. BABCOCK, G.T., OXYGEN ACTIVATION AND THE CONSERVATION OF ENERGY IN CELL RESPIRATION, NATURE 356: 301 (1992). · DOI
  6. BACKES, G, THE ENVIRONMENT OF FE4S4 CLUSTERS IN FERREDOXINS AND HIGH-POTENTIAL IRON PROTEINS - NEW INFORMATION FROM X-RAY CRYSTALLOGRAPHY AND RESONANCE RAMAN-SPECTROSCOPY, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 113: 2055 (1991). · DOI
  7. BARTON, DHR, THE SELECTIVE FUNCTIONALIZATION OF SATURATED-HYDROCARBONS - GIF CHEMISTRY, ACCOUNTS OF CHEMICAL RESEARCH 25: 504 (1992). · DOI
  8. BEESE, L.S., STRUCTURAL BASIS FOR THE 3'-5' EXONUCLEASE ACTIVITY OF ESCHERICHIA-COLI DNA-POLYMERASE-I - A 2 METAL-ION MECHANISM, EMBO JOURNAL 10: 25 (1991). · DOI · Paper page
  9. BEINERT, H, 3-IRON CLUSTERS IN IRON SULFUR PROTEINS, ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 222: 333 (1983). · DOI
  10. BEINERT, H, RECENT DEVELOPMENTS IN THE FIELD OF IRON-SULFUR PROTEINS, FASEB JOURNAL 4: 2483 (1990). · DOI
  11. 10.1126/science.1334572 · DOI
  12. BLACKBURN, N.J., X-RAY ABSORPTION STUDIES OF 3-COORDINATE DICOPPER(I) COMPLEXES AND THEIR DIOXYGEN ADDUCTS, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 110: 4263 (1988). · DOI
  13. BOLIN, J.T., THE UNUSUAL METAL-CLUSTERS OF NITROGENASE - STRUCTURAL FEATURES REVEALED BY X-RAY ANOMALOUS DIFFRACTION STUDIES OF THE MOFE PROTEIN FROM CLOSTRIDIUM-PASTEURIANUM, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 90: 1078 (1993).
  14. BOLLINGER, J.M., NOVEL DIFERRIC RADICAL INTERMEDIATE RESPONSIBLE FOR TYROSYL RADICAL FORMATION IN ASSEMBLY OF THE COFACTOR OF RIBONUCLEOTIDE REDUCTASE, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 113: 6289 (1991). · DOI
  15. 10.1126/science.1650033 · DOI
  16. 10.1126/science.7123255 · DOI
  17. Bruice, T. C., Biomimetic Chemistry 191: 89 (1980). · DOI
  18. BURGESON, I.E., SELECTIVE HYDROLYSIS OF UNACTIVATED PEPTIDE-BONDS, PROMOTED BY PLATINUM(II) COMPLEXES ANCHORED TO AMINO-ACID SIDE-CHAINS, INORGANIC CHEMISTRY 30: 4299 (1991). · DOI
  19. BURLEY, S.K., MOLECULAR-STRUCTURE OF LEUCINE AMINOPEPTIDASE AT 2.7-A RESOLUTION, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 87: 6878 (1990).
  20. BURLEY, S.K., LEUCINE AMINOPEPTIDASE - BESTATIN INHIBITION AND A MODEL FOR ENZYME-CATALYZED PEPTIDE HYDROLYSIS, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 88: 6916 (1991).
  21. Butler, A., Bioinorganic Catalysis: 425 (1993).
  22. CAMMACK, R, IRON-SULFUR CLUSTERS IN ENZYMES - THEMES AND VARIATIONS, ADVANCES IN INORGANIC CHEMISTRY 38: 281 (1992). · DOI
  23. Cammack, R., Bioinorganic Catalysis: 189 (1993).
  24. 10.1126/science.8484118 · DOI · Paper page
  25. Chan, S. I., Bioinorganic Chemistry of Copper: 184 (1993).
  26. CHAUDHURI, P, [L2FE-2(II)(MU-OH)(MU-CH3CO2)2](CLO4).H2O, A MODEL-COMPOUND FOR THE DIIRON CENTERS IN DEOXYHEMERYTHRIN, ANGEWANDTE CHEMIE-INTERNATIONAL EDITION IN ENGLISH 24: 778 (1985). · DOI
  27. CHIN, J, DEVELOPING ARTIFICIAL HYDROLYTIC METALLOENZYMES BY A UNIFIED MECHANISTIC APPROACH, ACCOUNTS OF CHEMICAL RESEARCH 24: 145 (1991). · DOI
  28. CHIOU, Y.M., MODEL COMPLEXES FOR ALPHA-KETO ACID-DEPENDENT ENZYMES - STRUCTURE AND REACTIVITY OF (FE(II)[TRIS[(6-METHYL-2-PYRIDYL)METHYL]AMINE](BENZOYL-FORMATE))(CLO4), JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 114: 7567 (1992). · DOI
  29. CHRISTIANSON, D.W., STRUCTURAL BIOLOGY OF ZINC, ADVANCES IN PROTEIN CHEMISTRY 42: 281 (1991). · DOI
  30. Christodoulou, D., Bioinorganic Chemistry of Copper: 427 (1993).
  31. CHRISTODOULOU, D, JOURNAL OF THE CHEMICAL SOCIETY-CHEMICAL COMMUNICATIONS: 937 (1993).
  32. COLEMAN, J.E., ZINC PROTEINS - ENZYMES, STORAGE PROTEINS, TRANSCRIPTION FACTORS, AND REPLICATION PROTEINS, ANNUAL REVIEW OF BIOCHEMISTRY 61: 897 (1992). · DOI · Paper page
  33. Collman, J. P., Metal Ion Activation of Dioxygen: 1 (1980).
  34. COOPERMAN, B.S., EVOLUTIONARY CONSERVATION OF THE ACTIVE-SITE OF SOLUBLE INORGANIC PYROPHOSPHATASE, TRENDS IN BIOCHEMICAL SCIENCES 17: 262 (1992). · DOI
  35. COUCOUVANIS, D, ACCOUNTS OF CHEMICAL RESEARCH 24: 1 (1991). · DOI
  36. 10.1126/science.3358128 · DOI · Paper page
  37. DAY, E.P., SATURATION MAGNETIZATION OF UREASES FROM KLEBSIELLA-AEROGENES AND JACK BEAN - NO EVIDENCE FOR EXCHANGE COUPLING BETWEEN THE 2 ACTIVE-SITE NICKEL IONS IN THE NATIVE ENZYMES, INORGANIC CHEMISTRY 32: 634 (1993). · DOI
  38. DEGRADO, W.F., CURR OPIN STRUC BIOL 1: 984 (1991). · DOI
  39. DEMONTELLANO, PRO, CONTROL OF THE CATALYTIC ACTIVITY OF PROSTHETIC HEME BY THE STRUCTURE OF HEMOPROTEINS, ACCOUNTS OF CHEMICAL RESEARCH 20: 289 (1987). · DOI
  40. DEWITT, J.G., X-RAY ABSORPTION, MOSSBAUER, AND EPR STUDIES OF THE DINUCLEAR IRON CENTER IN THE HYDROXYLASE COMPONENT OF METHANE MONOOXYGENASE, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 113: 9219 (1991). · DOI
  41. Dismukes, G. C., Bioinorganic Catalysis: 317 (1993).
  42. DONG, Y.H., DIOXYGEN BINDING TO DIFERROUS CENTERS - MODELS FOR DIIRON OXO PROTEINS, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 115: 1851 (1993). · DOI
  43. DRGO, R.S., COORDIN CHEM REV 117: 185 (1992). · DOI
  44. EMPTAGE, M.H., ACONITASE - EVOLUTION OF THE ACTIVE-SITE PICTURE, ACS SYMPOSIUM SERIES 372: 343 (1988). · DOI
  45. ERMACORA, M.R., CONFORMATION-DEPENDENT CLEAVAGE OF STAPHYLOCOCCAL NUCLEASE WITH A DISULFIDE-LINKED IRON CHELATE, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 89: 6383 (1992).
  46. Evans, D. J., Bioinorganic Catalysis: 89 (1983).
  47. Fee, J. A., Bioinorganic Chemistry of Copper: 485 (1993).
  48. Fenton, D. E., Journal of the Chemical Society, Dalton Transactions 1993: 1349 (1993).
  49. FIFE, T. H., PERSPECTIVES ON BIOINORGANIC CHEMISTRY 1: 43 (1991).
  50. FONTECAVE, M, THE REDOX CENTERS OF RIBONUCLEOTIDE REDUCTASE OF ESCHERICHIA-COLI, ADVANCES IN ENZYMOLOGY AND RELATED AREAS OF MOLECULAR BIOLOGY 65: 147 (1992).
  51. Fox, B. G., Biological Oxidation Systems 1: 367 (1990).
  52. FREEMAN, J.C., REDOX CYCLING OF ENZYME-BOUND COPPER DURING PEPTIDE AMIDATION, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 115: 4923 (1993). · DOI
  53. 10.1126/science.1529353 · DOI · Paper page
  54. GHISLA, S, MECHANISMS OF FLAVOPROTEIN-CATALYZED REACTIONS, EUROPEAN JOURNAL OF BIOCHEMISTRY 181: 1 (1989). · DOI · Paper page
  55. GOLDBERG, D.P., COMPLEXES OF A PENDANT PHENOXYL RADICAL LIGAND, INCLUDING A NEW MODEL FOR THE RIBONUCLEOTIDE REDUCTASE R2-PROTEIN, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 115: 5346 (1993). · DOI
  56. GUNTER, M. J., COORDINATION CHEMISTRY REVIEWS 108: 115 (1991). · DOI
  57. HAILE, D.J., PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 89: 7546 (1992).
  58. HAN, H, ROLE OF DIVALENT-CATIONS IN THE 3',5'-EXONUCLEASE REACTION OF DNA-POLYMERASE-I, BIOCHEMISTRY 30: 11104 (1991). · DOI
  59. HANSEN, S, CRYSTAL-STRUCTURES OF PHOSPHATE, IODIDE AND IODATE-INHIBITED PHOSPHOLIPASE-C FROM BACILLUS-CEREUS AND STRUCTURAL INVESTIGATIONS OF THE BINDING OF REACTION-PRODUCTS AND A SUBSTRATE-ANALOG, JOURNAL OF MOLECULAR BIOLOGY 225: 543 (1992). · DOI
  60. HARRISON, P.M., PROBING STRUCTURE-FUNCTION RELATIONS IN FERRITIN AND BACTERIOFERRITIN, ADVANCES IN INORGANIC CHEMISTRY 36: 449 (1991). · DOI
  61. HAYASHI, Y, CHEMISTRY LETTERS: 91 (1992).
  62. HENDRY, P, METAL-ION PROMOTED REACTIONS OF PHOSPHATE DERIVATIVES, PROGRESS IN INORGANIC CHEMISTRY 38: 201 (1990).
  63. HILL, H. A. O., CHEM BRIT: 119 (1976).
  64. HOFFMAN, B.M., LONG-RANGE ELECTRON-TRANSFER WITHIN METAL-SUBSTITUTED PROTEIN COMPLEXES, STRUCTURE AND BONDING 75: 85 (1991). · DOI
  65. HOLM, R. H., ADVANCES IN INORGANIC CHEMISTRY 38: 1 (1992). · DOI
  66. HOLM, R.H., SUBSITE-SPECIFIC STRUCTURES AND REACTIONS IN NATIVE AND SYNTHETIC (4FE-4S) CUBANE-TYPE CLUSTERS, PROGRESS IN INORGANIC CHEMISTRY 38: 1 (1990).
  67. HOLMES, M.A., STRUCTURES OF DEOXY AND OXY HEMERYTHRIN AT 2.0-A RESOLUTION, JOURNAL OF MOLECULAR BIOLOGY 218: 583 (1991). · DOI
  68. HOUGH, E, HIGH-RESOLUTION (1.5 A) CRYSTAL-STRUCTURE OF PHOSPHOLIPASE-C FROM BACILLUS-CEREUS, NATURE 338: 357 (1989). · DOI · Paper page
  69. HOWARD, J.B., PERSPECTIVES ON NONHEME IRON PROTEIN CHEMISTRY, ADVANCES IN PROTEIN CHEMISTRY 42: 199 (1991). · DOI
  70. 10.1126/science.7384796 · DOI
  71. IGNARRO, L.J., HEME-DEPENDENT ACTIVATION OF GUANYLATE-CYCLASE BY NITRIC-OXIDE - A NOVEL SIGNAL TRANSDUCTION MECHANISM, BLOOD VESSELS 28: 67 (1991).
  72. Ingraham, L. I., Biochemistry of the Elements 4: 157 (1985).
  73. JACOBSON, R.R., A CU2-O2 COMPLEX - CRYSTAL-STRUCTURE AND CHARACTERIZATION OF A REVERSIBLE DIOXYGEN BINDING SYSTEM, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 110: 3690 (1988). · DOI
  74. Karlin, K. D., Bioinorganic Catalysis: 261 (1993).
  75. Karlin K. D. Bioinorganic Chemistry of Copper (1993). · DOI · Paper page
  76. KARLIN, K.D., COPPER-MEDIATED HYDROXYLATION OF AN ARENE - MODEL SYSTEM FOR THE ACTION OF COPPER MONOOXYGENASES - STRUCTURES OF A BINUCLEAR CU(I) COMPLEX AND ITS OXYGENATED PRODUCT, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 106: 2121 (1984). · DOI · Paper page
  77. KENNEDY, M.C., ACONITASE - AN IRON-SULFUR ENZYME, ADVANCES IN INORGANIC CHEMISTRY 38: 323 (1992). · DOI
  78. KENNEDY, M.C., PURIFICATION AND CHARACTERIZATION OF CYTOSOLIC ACONITASE FROM BEEF-LIVER AND ITS RELATIONSHIP TO THE IRON-RESPONSIVE ELEMENT BINDING-PROTEIN, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 89: 11730 (1992).
  79. KIM, E.E., REACTION-MECHANISM OF ALKALINE-PHOSPHATASE BASED ON CRYSTAL-STRUCTURES - 2-METAL ION CATALYSIS, JOURNAL OF MOLECULAR BIOLOGY 218: 449 (1991). · DOI
  80. 10.1038/360553a0 · DOI · Paper page
  81. KIMURA, E, A ZINC(II) COMPLEX OF 1,5,9-TRIAZACYCLODODECANE ([12]ANEN3) AS A MODEL FOR CARBONIC-ANHYDRASE, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 112: 5805 (1990). · DOI
  82. KIMURA, E, Macrocyclic Polyamine Zinc(II) Complexes as Advanced Models for Zinc(II) Enzymes, PROGRESS IN INORGANIC CHEMISTRY 41: 443 (1993).
  83. KITAJIMA, N, SYNTHETIC APPROACH TO THE STRUCTURE AND FUNCTION OF COPPER PROTEINS, ADVANCES IN INORGANIC CHEMISTRY 39: 1 (1992). · DOI
  84. KITAJIMA, N, MU-ETA-2-ETA-2-PEROXO BINUCLEAR COPPER COMPLEX, [CU(HB(3,5-IPR2PZ)3)]2(O2), JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 111: 8975 (1989). · DOI · Paper page
  85. KITAJIMA, N, SYNTHETIC MODEL FOR DIOXYGEN BINDING-SITES OF NONHEME IRON PROTEINS - X-RAY STRUCTURE OF FE(OBZ)(MECN)(HB(3,5-IPR2PZ)3) AND RESONANCE RAMAN EVIDENCE FOR REVERSIBLE FORMATION OF A PEROXO ADDUCT, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 112: 6402 (1990). · DOI
  86. KITAJIMA, N, A NEW MODEL FOR DIOXYGEN BINDING IN HEMOCYANIN - SYNTHESIS, CHARACTERIZATION, AND MOLECULAR-STRUCTURE OF THE MU-ETA-2-ETA-2 PEROXO DINUCLEAR COPPER(II) COMPLEXES, [CU(HB(3,5-R2PZ)3)]2(O2) (R = ISO-PR AND PH), JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 114: 1277 (1992). · DOI
  87. KOLODZIEJ, A. F., The Chemistry of Nickel-Containing Enzymes, PROGRESS IN INORGANIC CHEMISTRY 41: 493 (1993).
  88. Kovacs, J. A., Models in Inorganic Biochemistry 9: 173 (1993).
  89. 10.1126/science.1411536 · DOI · Paper page
  90. KURTZ, D.M., OXO-BRIDGED AND HYDROXO-BRIDGED DIIRON COMPLEXES - A CHEMICAL PERSPECTIVE ON A BIOLOGICAL UNIT, CHEMICAL REVIEWS 90: 585 (1990). · DOI · Paper page
  91. LEE, S.C., A SYNTHETIC ANALOG OF THE IRON COPPER BRIDGED ASSEMBLY IN CYTOCHROME-C-OXIDASE, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 115: 5833 (1993). · DOI
  92. LEGALL, J, ISOLATION AND CHARACTERIZATION OF RUBRERYTHRIN, A NON-HEME IRON PROTEIN FROM DESULFOVIBRIO-VULGARIS THAT CONTAINS RUBREDOXIN CENTERS AND A HEMERYTHRIN-LIKE BINUCLEAR IRON CLUSTER, BIOCHEMISTRY 27: 1636 (1988). · DOI
  93. LEISING, R.A., MODELS FOR NONHEME IRON OXYGENASES - A HIGH-VALENT IRON OXO INTERMEDIATE, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 113: 3988 (1991). · DOI
  94. LINDAHL, P. A., JOURNAL OF CLUSTER SCIENCE 1: 29 (1990). · DOI
  95. LIPPARD, S.J., OXO-BRIDGED POLYIRON CENTERS IN BIOLOGY AND CHEMISTRY, ANGEWANDTE CHEMIE-INTERNATIONAL EDITION IN ENGLISH 27: 344 (1988). · DOI
  96. LIPPARD, S. J., PROGRESS IN INORGANIC CHEMISTRY 18: v (1973).
  97. LIU, K.E., RADICAL CLOCK SUBSTRATE PROBES AND KINETIC ISOTOPE EFFECT STUDIES OF THE HYDROXYLATION OF HYDROCARBONS BY METHANE MONOOXYGENASE, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 115: 939 (1993). · DOI
  98. Magnus, K. A., Bioinorganic Chemistry of Copper: 143 (1993).
  99. MARLETTA, M.A., BIOFACTORS 2: 219 (1990).
  100. MARONEY, M.J., EXAFS INVESTIGATIONS OF THE NI SITE IN THIOCAPSA-ROSEOPERSICINA HYDROGENASE - EVIDENCE FOR A NOVEL NI,FE,S CLUSTER, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 113: 3962 (1991). · DOI
  101. Marzilli, L. G., Bioinorganic Catalysis: 227 (1993).
  102. MATHEWS, F.S., CURR OPIN STRUC BIOL 1: 954 (1991). · DOI
  103. MATTHEWS, B. W., ACCOUNTS OF CHEMICAL RESEARCH 21: 333 (1988). · DOI · Paper page
  104. MCLENDON, G, INTERPROTEIN ELECTRON-TRANSFER, CHEMICAL REVIEWS 92: 481 (1992). · DOI
  105. MCLENDON, G, THERMODYNAMIC AND KINETIC ASPECTS OF BINDING AND RECOGNITION IN THE CYTOCHROME-C CYTOCHROME-C PEROXIDASE COMPLEX, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 115: 3665 (1993). · DOI
  106. MCREE, D.E., THE HEME AND FE4S4 CLUSTER IN THE CRYSTALLOGRAPHIC STRUCTURE OF ESCHERICHIA-COLI SULFITE REDUCTASE, JOURNAL OF BIOLOGICAL CHEMISTRY 261: 10277 (1986). · DOI
  107. MENIEUR, B, CHEM REV 92: 1411 (1992). · DOI · Paper page
  108. 10.1038/355796a0 · DOI · Paper page
  109. MOURA, I, DIRECT SPECTROSCOPIC EVIDENCE FOR THE PRESENCE OF A 6FE CLUSTER IN AN IRON-SULFUR PROTEIN ISOLATED FROM DESULFOVIBRIO-DESULFURICANS (ATCC-27774), JOURNAL OF BIOLOGICAL CHEMISTRY 267: 4489 (1992). · DOI
  110. MULLIEZ, E, AN IRON-SULFUR CENTER AND A FREE-RADICAL IN THE ACTIVE ANAEROBIC RIBONUCLEOTIDE REDUCTASE OF ESCHERICHIA-COLI, JOURNAL OF BIOLOGICAL CHEMISTRY 268: 2296 (1993). · DOI
  111. Nanthakumar, A., Journal of the American Chemical Society 115: 8513 (1993). · DOI
  112. NASIR, M.S., MECHANISM OF AROMATIC HYDROXYLATION IN A COPPER MONOOXYGENASE MODEL SYSTEM - 1,2-METHYL MIGRATIONS AND THE NIH SHIFT IN COPPER CHEMISTRY, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 114: 2482 (1992). · DOI
  113. NORDLUND, P, THE ACTIVE-SITE STRUCTURE OF METHANE MONOOXYGENASE IS CLOSELY RELATED TO THE BINUCLEAR IRON CENTER OF RIBONUCLEOTIDE REDUCTASE, FEBS LETTERS 307: 257 (1992). · DOI
  114. NORDLUND, P, 3-DIMENSIONAL STRUCTURE OF THE FREE-RADICAL PROTEIN OF RIBONUCLEOTIDE REDUCTASE, NATURE 345: 593 (1990). · DOI · Paper page
  115. 10.1126/science.8342038 · DOI
  116. 10.1126/science.1529351 · DOI
  117. OSTOVIC, D, MECHANISM OF ALKENE EPOXIDATION BY IRON, CHROMIUM, AND MANGANESE HIGHER VALENT OXO-METALLOPORPHYRINS, ACCOUNTS OF CHEMICAL RESEARCH 25: 314 (1992). · DOI
  118. 10.1126/science.1334573 · DOI · Paper page
  119. PERUTZ, M.F., REGULATION OF OXYGEN-AFFINITY OF HEMOGLOBIN - INFLUENCE OF STRUCTURE OF THE GLOBIN ON THE HEME IRON, ANNUAL REVIEW OF BIOCHEMISTRY 48: 327 (1979). · DOI · Paper page
  120. PESSI, A, A DESIGNED METAL-BINDING PROTEIN WITH A NOVEL FOLD, NATURE 362: 367 (1993). · DOI
  121. Pilato, R. S., Bioinorganic Catalysis: 131 (1993).
  122. POULOS, T.L., CYTOCHROME-P450CAM - CRYSTALLOGRAPHY, OXYGEN ACTIVATION, AND ELECTRON-TRANSFER, FASEB JOURNAL 6: 674 (1992). · DOI
  123. POYNER, R.R., STRUCTURE OF THE BIS DIVALENT-CATION COMPLEX WITH PHOSPHONOACETOHYDROXAMATE AT THE ACTIVE-SITE OF ENOLASE, BIOCHEMISTRY 31: 7166 (1992). · DOI
  124. PRINCE, R.C., RISING INTEREST IN NITRIC-OXIDE SYNTHASE, TRENDS IN BIOCHEMICAL SCIENCES 18: 35 (1993). · DOI
  125. Que L Metal Clusters in Proteins: (1988). · DOI
  126. Que, L., Bioinorganic Catalysis: 347 (1993).
  127. QUE, L, PROGRESS IN INORGANIC CHEMISTRY 38: 97 (1990).
  128. QUIOCHO, F.A., PROTEIN ENGINEERING - MAKING OF THE MINIBODY, NATURE 362: 293 (1993). · DOI
  129. RAGSDALE, S.W., ENZYMOLOGY OF THE ACETYL-COA PATHWAY OF CO2 FIXATION, CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY 26: 261 (1991). · DOI · Paper page
  130. RANA, T.M., IRON CHELATE MEDIATED PROTEOLYSIS - PROTEIN-STRUCTURE DEPENDENCE, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 113: 1859 (1991). · DOI
  131. RARDIN, R.L., MONODENTATE CARBOXYLATE COMPLEXES AND THE CARBOXYLATE SHIFT - IMPLICATIONS FOR POLYMETALLOPROTEIN STRUCTURE AND FUNCTION, NEW JOURNAL OF CHEMISTRY 15: 417 (1991).
  132. RECZKOWSKI, R.S., EPR EVIDENCE FOR BINUCLEAR MN(II) CENTERS IN RAT-LIVER ARGINASE, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 114: 10992 (1992). · DOI
  133. 10.1126/science.8511586 · DOI
  134. RODERICK, S.L., STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA-COLI - A NEW TYPE OF PROTEOLYTIC-ENZYME, BIOCHEMISTRY 32: 3907 (1993). · DOI · Paper page
  135. SANDERSLOEHR, J, ELECTRONIC AND RAMAN-SPECTROSCOPIC PROPERTIES OF OXO-BRIDGED DINUCLEAR IRON CENTERS IN PROTEINS AND MODEL COMPOUNDS, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 111: 8084 (1989). · DOI
  136. 10.1021/cen-v068n018.p026 · DOI
  137. SILVERMAN, D.N., THE CATALYTIC MECHANISM OF CARBONIC-ANHYDRASE - IMPLICATIONS OF A RATE-LIMITING PROTOLYSIS OF WATER, ACCOUNTS OF CHEMICAL RESEARCH 21: 30 (1988). · DOI · Paper page
  138. SNYDER, S.H., BIOLOGICAL ROLES OF NITRIC-OXIDE, SCIENTIFIC AMERICAN 266: 68 (1992).
  139. SOLOMON, E.I., THE ELECTRONIC-STRUCTURES OF ACTIVE-SITES IN NONHEME IRON ENZYMES, ACCOUNTS OF CHEMICAL RESEARCH 25: 343 (1992). · DOI
  140. SOLOMON, E.I., ELECTRONIC-STRUCTURES OF ACTIVE-SITES IN COPPER PROTEINS - CONTRIBUTIONS TO REACTIVITY, CHEMICAL REVIEWS 92: 521 (1992). · DOI · Paper page
  141. 10.1126/science.8384374 · DOI · Paper page
  142. STEPHENS, T, J NIH RES 3: 21 (1991).
  143. STEWART, L.C., DOPAMINE BETA-HYDROXYLASE OF ADRENAL CHROMAFFIN GRANULES - STRUCTURE AND FUNCTION, ANNUAL REVIEW OF BIOCHEMISTRY 57: 551 (1988). · DOI
  144. STUBBE, J, CURR OPIN STRUC BIOL 1: 788 (1991). · DOI
  145. STUBBE, J.A., PROTEIN RADICAL INVOLVEMENT IN BIOLOGICAL CATALYSIS, ANNUAL REVIEW OF BIOCHEMISTRY 58: 257 (1989). · DOI
  146. STUBBE, J.A., RIBONUCLEOTIDE REDUCTASES - AMAZING AND CONFUSING, JOURNAL OF BIOLOGICAL CHEMISTRY 265: 5329 (1990). · DOI · Paper page
  147. SUH, J.H., MODEL STUDIES OF METALLOENZYMES INVOLVING METAL-IONS AS LEWIS ACID CATALYSTS, ACCOUNTS OF CHEMICAL RESEARCH 25: 273 (1992). · DOI
  148. SUSLICK, K.S., THE SYNTHETIC ANALOGS OF O-2-BINDING HEME-PROTEINS, JOURNAL OF CHEMICAL EDUCATION 62: 974 (1985). · DOI
  149. 10.1126/science.8446898 · DOI
  150. TAINER, J. A., CURRENT OPINION IN BIOTECHNOLOGY 3: 378 (1992). · DOI
  151. THEIL, E.C., THE FERRITIN FAMILY OF IRON STORAGE PROTEINS, ADVANCES IN ENZYMOLOGY AND RELATED AREAS OF MOLECULAR BIOLOGY 63: 421 (1990).
  152. 10.1126/science.251.4996.932 · DOI · Paper page
  153. TRAYLOR, T.G., NITRIC OXIDE-TRIGGERED HEME-MEDIATED HYDROLYSIS - A POSSIBLE MODEL FOR BIOLOGICAL REACTIONS OF NO, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 115: 810 (1993). · DOI
  154. TRAYLOR, T.G., KINETICS AND MECHANISM STUDIES IN BIOMIMETIC CHEMISTRY - METALLOENZYME MODEL SYSTEMS, PURE AND APPLIED CHEMISTRY 63: 265 (1991). · DOI
  155. TYEKLAR, Z, REVERSIBLE-REACTION OF O2 (AND CO) WITH A COPPER(I) COMPLEX - X-RAY STRUCTURES OF RELEVANT MONONUCLEAR CU(I) PRECURSOR ADDUCTS AND THE TRANS-(MU-1,2-PEROXO)DICOPPER(II) PRODUCT, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 115: 2677 (1993). · DOI
  156. VALLEE, B.L., ZINC COORDINATION, FUNCTION, AND STRUCTURE OF ZINC ENZYMES AND OTHER PROTEINS, BIOCHEMISTRY 29: 5647 (1990). · DOI
  157. VALLEE, B.L., NEW PERSPECTIVE ON ZINC BIOCHEMISTRY - COCATALYTIC SITES IN MULTI-ZINC ENZYMES, BIOCHEMISTRY 32: 6493 (1993). · DOI
  158. VINCENT, J.B., PROTEINS CONTAINING OXO-BRIDGED DINUCLEAR IRON CENTERS - A BIOINORGANIC PERSPECTIVE, CHEMICAL REVIEWS 90: 1447 (1990). · DOI
  159. VINCENT, J.B., HYDROLYSIS OF PHOSPHATE MONOESTERS - A BIOLOGICAL PROBLEM WITH MULTIPLE CHEMICAL SOLUTIONS, TRENDS IN BIOCHEMICAL SCIENCES 17: 105 (1992). · DOI
  160. VOLBEDA, A, CRYSTAL-STRUCTURE OF PENICILLIUM-CITRINUM P1 NUCLEASE AT 2.8-A RESOLUTION, EMBO JOURNAL 10: 1607 (1991). · DOI · Paper page
  161. 10.1126/science.7678352 · DOI
  162. Watanabe, Y., Mechanisms of Catalysis 20: 405 (1992).
  163. WHITE, K.A., NITRIC-OXIDE SYNTHASE IS A CYTOCHROME-P-450 TYPE HEMOPROTEIN, BIOCHEMISTRY 31: 6627 (1992). · DOI · Paper page
  164. WIEGHARDT, K, [((C6H15N3)FE)2(MU-O)(MU-CH3CO2)2]2+, A DINUCLEAR IRON(III) COMPLEX WITH A METAZIDOHEMERYTHRIN-TYPE STRUCTURE, ANGEWANDTE CHEMIE-INTERNATIONAL EDITION IN ENGLISH 22: 727 (1983). · DOI
  165. WUENSCHELL, G.E., H-BONDED OXYHEMOGLOBIN MODELS WITH SUBSTITUTED PICKET-FENCE PORPHYRINS - THE MODEL-COMPOUND EQUIVALENT OF SITE-DIRECTED MUTAGENESIS, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 114: 3346 (1992). · DOI
  166. ZANG, Y, A HIGH-POTENTIAL FERROUS COMPLEX AND ITS CONVERSION TO AN ALKYLPEROXOIRON(III) INTERMEDIATE - A LIPOXYGENASE MODEL, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 115: 811 (1993). · DOI
  167. 10.1126/science.8100368 · DOI · Paper page

Cited by

See all 554

Metadata

Authors
Karlin, K. D.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1993-08-06
Volume
261
Issue
5122
Pages
701-708
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.7688141
OpenAlex
W2071894609
Cited by
554
References
4
FWCI
23.84
Type
journal article
Language
en
Open access
closed

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.