Diversity and conservation of interactions for binding heme in b-type heme proteins.

Covering: up to 2006The heme prosthetic group is vital to many cellular processes and is therefore widespread throughout organisms of different phylogenetic origin. Heme is used in proteins involved in cellular respiration, acts as a chemical mediator in ligand binding and signalling proteins, and is the key co-factor in many enzymes. Strikingly, there are over 20 different folding topologies of b-type heme proteins that are able to incorporate the same, chemically identical heme ligand. Comparisons of structures show that heme–protein interactions are generally diverse, though a degree of conservation exists at contacts with the pyrrole rings, the propionate groups and the proximal ligand. These interaction “hot spots” presumably define major determinants for binding heme and provide guidelines for the future design of novel heme proteins.

[1]  J Deisenhofer,et al.  Structure and function of cytochromes P450: a comparative analysis of three crystal structures. , 1995, Structure.

[2]  R. Farid,et al.  Design, synthesis, and characterization of a novel hemoprotein , 2001, Protein science : a publication of the Protein Society.

[3]  P. Dutton,et al.  Histidine placement in de novo–designed heme proteins , 1999, Protein science : a publication of the Protein Society.

[4]  R. Hunt,et al.  Hemopexin joins transferrin as representative members of a distinct class of receptor-mediated endocytic transport systems. , 1990, European journal of cell biology.

[5]  D. Rees,et al.  Molecular Basis of Sulfite Oxidase Deficiency from the Structure of Sulfite Oxidase , 1997, Cell.

[6]  G. McGaughey,et al.  pi-Stacking interactions. Alive and well in proteins. , 1998, The Journal of biological chemistry.

[7]  S. Sligar,et al.  Interpretation of hyperfine shift patterns in ferricytochromes b5 in terms of angular position of the heme: a sensitive probe for peripheral heme protein interactions. , 1993, Biochimica et biophysica acta.

[8]  M. M. Fitzgerald,et al.  Construction of a bisaquo heme enzyme and binding by exogenous ligands. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[9]  P. Leslie Dutton,et al.  Design of a heme-binding four-helix bundle , 1994 .

[10]  N. Sinha,et al.  Why isn't 'standard' heme good enough for c-type and d1-type cytochromes? , 2005, Dalton transactions.

[11]  P. Weber,et al.  Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation , 1999, Nature Structural Biology.

[12]  Elizabeth M. Boon,et al.  Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[13]  Jon Marles-Wright,et al.  Structure-function relationships in heme-proteins. , 2002, DNA and cell biology.

[14]  B. R. Gibney,et al.  Effect of four helix bundle topology on heme binding and redox properties. , 1998, Biochemistry.

[15]  D. J. Schuller,et al.  Structure of the CO sensing transcription activator CooA , 2000, Nature Structural Biology.

[16]  J. Zou,et al.  Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.

[17]  Collaborative Computational,et al.  The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.

[18]  G Vriend,et al.  WHAT IF: a molecular modeling and drug design program. , 1990, Journal of molecular graphics.

[19]  Hydrogen-bond and deprotonation effects on the resonance Raman iron-imidazole mode in deoxyhemoglobin models: implications for hemoglobin cooperativity , 1980 .

[20]  Christopher C. Moser,et al.  Design and synthesis of multi-haem proteins , 1994, Nature.

[21]  M. Brunori,et al.  The structure of murine neuroglobin: Novel pathways for ligand migration and binding , 2004, Proteins.

[22]  J. Andersen,et al.  Crystal structures of a nitric oxide transport protein from a blood-sucking insect , 1998, Nature Structural Biology.

[23]  J B Findlay,et al.  Promise: a new database of information on prosthetic centres and metal ions in protein active sites. , 1997, Protein engineering.

[24]  M C Peitsch,et al.  Protein modelling for all. , 1999, Trends in biochemical sciences.

[25]  P. Strittmatter,et al.  The effect of heme binding on the tryptophan residue and the protein conformation of cytochrome b 5 . , 1972, The Journal of biological chemistry.

[26]  Anne Lecroisey,et al.  The crystal structure of HasA, a hemophore secreted by Serratia marcescens , 1999, Nature Structural Biology.

[27]  B. Mikami,et al.  A Redox-controlled Molecular Switch Revealed by the Crystal Structure of a Bacterial Heme PAS Sensor* , 2004, Journal of Biological Chemistry.

[28]  W. Pfeil.  Thermodynamics of apocytochrome b5 unfolding , 1993, Protein science : a publication of the Protein Society.

[29]  L. H. Bradley,et al.  De novo proteins from designed combinatorial libraries , 2004, Protein science : a publication of the Protein Society.

[30]  A. Munro,et al.  Heme: The most versatile redox centre in biology? , 1997 .

[31]  D. Barrick,et al.  Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly. , 1994, Biochemistry.

[32]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1978, Archives of biochemistry and biophysics.

[33]  G. Mortuza,et al.  Mutagenesis of residues 27 and 78 modulates heme orientation in cytochrome b 5 , 1997, FEBS letters.

[34]  D. Carter,et al.  The atomic structure of human methemalbumin at 1.9 A. , 2002, Biochemical and biophysical research communications.

[35]  E. Liong,et al.  Waterproofing the Heme Pocket , 2001, The Journal of Biological Chemistry.

[36]  Edward N. Baker,et al.  Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains , 1999, Nature Structural Biology.

[37]  U. Samanta,et al.  Packing of aromatic rings against tryptophan residues in proteins. , 1999, Acta crystallographica. Section D, Biological crystallography.

[38]  C. Yan,et al.  The origin of differences in the physical properties of the equilibrium forms of cytochrome b5 revealed through high-resolution NMR structures and backbone dynamic analyses. , 1998, Biochemistry.

[39]  H. Mihara,et al.  Design, synthesis and peroxidase-like activity of 3alpha-helix proteins covalently bound to heme. , 2000, Bioorganic & medicinal chemistry letters.

[40]  F. Rabanal,et al.  Toward the Synthesis of a Photosynthetic Reaction Center Maquette: A Cofacial Porphyrin Pair Assembled between Two Subunits of a Synthetic Four-Helix Bundle Multiheme Protein , 1996 .