Direct evidence for a hydrogen bond to bound dioxygen in a myoglobin/hemoglobin model system and in cobalt myoglobin by pulse-EPR spectroscopy.

[1]  S. Stoll,et al.  Peak suppression in ESEEM spectra of multinuclear spin systems. , 2005, Journal of magnetic resonance.

[2]  F. Diederich,et al.  Synthesis of Dendritic Metalloporphyrins with Distal H-Bond Donors as Model Systems for Hemoglobin , 2005 .

[3]  D. Goldfarb,et al.  Spin distribution and the location of protons in paramagnetic proteins. , 2004, Annual review of biophysics and biomolecular structure.

[4]  C. Sunderland,et al.  Functional analogues of cytochrome c oxidase, myoglobin, and hemoglobin. , 2004, Chemical reviews.

[5]  F. Diederich,et al.  Dendritic Iron Porphyrins with a Tethered Axial Ligand as New Model Compounds for Heme Monooxygenases , 2002 .

[6]  B. Kräutler,et al.  A Continuous Wave and Pulse EPR and ENDOR Investigation of Oxygenated Co(II) Corrin Complexes , 2001 .

[7]  Gunnar Jeschke,et al.  Principles of pulse electron paramagnetic resonance , 2001 .

[8]  M. Rohrer,et al.  Pulsed EPR spectroscopy: biological applications. , 2001, Annual review of physical chemistry.

[9]  J. Lukin,et al.  NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[10]  Stu Borman AFRICAN AIDS TRAGEDY : PATENT RIGHTS VERSUS HUMAN RIGHTS , 1999 .

[11]  Mark A Miller,et al.  Refined Synthesis of 5-Substituted Dipyrromethanes , 1999 .

[12]  M. Chance,et al.  Electron Spin Echo Envelope Modulation and Extended X-ray Absorption Fine Structure Studies of Active Site Models of Oxygenated Cobalt-Substituted Hemoproteins: Correlating Electron-Nuclear Couplings and Metal−Ligand Bond Lengths , 1997 .

[13]  F. Diederich,et al.  Dendrimers with Porphyrin Cores: Synthetic Models for Globular Heme Proteins , 1997 .

[14]  M. Ikeda-Saito,et al.  High Resolution Crystal Structures of the Deoxy, Oxy, and Aquomet Forms of Cobalt Myoglobin* , 1996, The Journal of Biological Chemistry.

[15]  Stephen G. Sligar,et al.  Mechanisms of Ligand Recognition in Myoglobin , 1994 .

[16]  Christopher A. Reed,et al.  Synthetic Heme Dioxygen Complexes , 1994 .

[17]  Michael L. Quillin,et al.  High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. , 1994, Journal of molecular biology.

[18]  B. Hoffman,et al.  Quantitative studies of davies pulsed ENDOR , 1992 .

[19]  N. Yordanov Electron Magnetic Resonance of Disordered Systems (EMARDIS – 91): Proceedings of the International Workshop , 1991 .

[20]  F. Walker,et al.  EPR evidence for hydrogen bond donation to the terminal oxygen of cobalt-oxygen model compounds and cobalt oxymyoglobin , 1985 .

[21]  E Antonini,et al.  Preparation and properties of apohemoglobin and reconstituted hemoglobins. , 1981, Methods in enzymology.

[22]  T. Yonetani,et al.  Freezing induced change in ligand orientation in oxycobalt-myoglobin , 1980, Nature.

[23]  J. Chien,et al.  Electron paramagnetic resonance crystallography of 17O-enriched oxycobaltomyoglobin: stereoelectronic structure of the cobalt dioxygen system. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[24]  E. R. Davies,et al.  A new pulse endor technique , 1974 .

[25]  D. Petering,et al.  Coboglobins: oxygen-carrying cobalt-reconstituted hemoglobin and myoglobin. , 1970, Proceedings of the National Academy of Sciences of the United States of America.

[26]  T. Creighton Methods in Enzymology , 1968, The Yale Journal of Biology and Medicine.

[27]  L. Pauling,et al.  Nature of the Iron–Oxygen Bond in Oxyhæmoglobin , 1964, Nature.

[28]  Henry Tauber,et al.  Methods of Enzymology. , 1956 .