This page was last updated December 10 and will not be updated again until February 7, 2006.

Special Issue of the Journal of Inorganic Biochemistry on
High-valent iron in chemistry and biology

Expected date of publication: March, 2006

Guest Editor:  Abhik Ghosh


Dear colleagues,

I will not edit this page for some time as I will be traveling. Let me take this opportunity to thank you for your contributions and for bearing with my gentle tyranny as Guest Editor. At this point, there is little doubt that this will be an exciting and useful volume, when it is published in a very few months.

All the best for the holiday season and a happy new year 2006,

Abhik

E-mail list: awalker@u.arizona.edu, hiro@ims.ac.jp, paul.gardner@cchmc.org, christopher.schofield@chemistry.oxford.ac.uk, abhik@chem.uit.no, chuanhe@uchicago.edu, pawel@louisville.edu, lou@scripps.edu, mtg10@psu.edu, ckrebs@psu.edu, jonas.peters@gmail.com, edward.solomon@stanford.edu, wwnam@ewha.ac.kr, kurtz@chem.uga.edu, dpg@jhu.edu, ps@physto.se, jterner@mail1.vcu.edu, que@chem.umn.edu, P.R.Taylor@warwick.ac.uk, riordan@udel.edu, s-sligar@uiuc.edu, fridovich@biochem.duke.edu, tc1u@andrew.cmu.edu, k.k.andersson@imbv.uio.no, Roger.Guilard@u-bourgogne.fr, dawson@sc.edu, ziegler@uakron.edu, mnewcomb@addisoncw.com, dario@qi.fcen.uba.ar, giulietta.smulevich@unifi.it, jouve@ibs.fr, graham@staffmail.ed.ac.uk, kkadish@uh.edu, sunneychan@yahoo.com, neese@mpi-muelheim.mpg.de, kazunari@ms.ifoc.kyushu-u.ac.jp, guallarv@sbcglobal.net, jtgroves@princeton.edu, gary.brudvig@yale.edu, victor.batista@yale.edu, riordan@udel.edu, olson@bioc.rice.edu, ulf.ryde@teokem.lu.se, teizo@ims.ac.jp, ConradJ.SCI@mail.uovs.ac.za


Contributors (in alphabetical order) and approximate thematic order

Keynote reviews
1. Larry Que, Minnesota, Nonheme Fe^IVO intermediates, Accepted for publication
2. John T. Groves, Princeton, Fe^IVO reaction pathways, Running late

Status of protonated ferryl groups
3. Mike Green, Penn State University, Protonated ferryl intermediates, Accepted for publication
4. Kristoffer Andersson, Oslo, Crystal structures of heme-oxygen intermediates, Accepted for publication
5. Helene Jouve, Grenoble, Catalase intermediates, Accepted for publication
6. Jim Terner, Virginia Commonwealth U., with Avram Gold and Raymond Weiss, Resonance Raman studies of compound I intermediates, Accepted for publication
7. Abhik Ghosh, Electronic ménages a trois: an MO perspective of protonated ferryl intermediates, Accepted for publication

Heme proteins and models
8. Steve Sligar, Urbana-Champaign, The status of Compound I for the cytochromes P₄₅₀, Accepted for publication
9. John Dawson, South Carolina, cytochromes P₄₅₀ compound I (short communication), Running late
10. Martin Newcomb, Chicago, Compound I kinetics (regular paper), Accepted for publication
11. Hiroshi Fujii, IMS, ¹⁷O NMR of metal-oxo porphyrins (short communication), Accepted for publication
12. Paul Gardner, Cincinnati, The NO dioxygenase mechanism of hemoglobins, Accepted for publication
13. Graham Pettigrew, Edinburgh, Structure and mechanism in the bacterial cytochrome c peroxidases (review), Accepted for publication
14. Giuletta Smulevich, Firenze, Catalase-peroxidases (KatG), Accepted for publication

Nonheme metalloenzymes and models
15. Carsten Krebs, J. M. Bollinger, Penn State University, High-spin Fe^IVO intermediates, Running late
16. Terrence Collins and Eckard Münck, Carnegie Mellon, Iron(IV)-TAML and related systems, Accepted for publication
17. Abhik Ghosh, High-valent transition metal TAML complexes: The end of innocence? Accepted for publication
18. Wonwoo Nam, Ewha Womans University, Metal-oxo intermediates, Accepted for publication
19. Jonas Peters, Caltech, Iron-imido/nitrido complexes, Running late
20. Christopher Schofield, Oxford, Crystallographic analyses of 2-oxoglutarate-dependent and related oxygenases, Accepted for publication
21. Chuan He, Chicago, New functions of nonheme iron: Focus on the DNA repair enzyme Alk B, Accepted for publication
22. Don Kurtz, University of Georgia, Avoiding high-valent iron intermediates: superoxide reductase and rubrerythrin, Accepted for publication
23. Irwin Fridovich, Duke University, SOD1-H₂O₂ interactions: role of carbonate radicals, Accepted for publication

Electronic structure and theory
24. Ed Solomon, Stanford, Electronic spectroscopy of mono- and binuclear high-valent iron sites, Accepted for publication
25. Lou Noodleman, Scripps, San Diego, High-valent diiron-oxo intermediates: connecting structure and spectroscopy, Accepted for publication
26. Abhik Ghosh, Tromsø, Norway, Nonheme iron and manganese oxo complexes, Accepted for publication
27. Peter Taylor, Warwick, UK, Highest-level ab initio modeling of MMO compound Q, Accepted for publication
28. Frank Neese, Mülheim, Germany, Multireference ab initio studies of Fe^IVO intermediates, Accepted for publication
29. Per Siegbahn, Stockholm, Enzyme mechanisms involving high-valent iron intermediates, Accepted for publication
30. Pawel Kozlowski, Kentucky, USA, and Teizo Kitagawa, IMS, Japan, Excited states of high-valent Fe porphyrins, Accepted for publication
31. Kazunari Yoshizawa, Japan, Axial ligand effects on compound I models, Accepted for publication
32. Victor Guallar, St. Louis, USA, QM/MM studies of Compound I, Accepted for publication
33. Dario Estrin, Buenos Aires, Heme-dioxygen modeling, Accepted for publication

Porphyrin analogs
34. F. Ann Walker, U. of Arizona, Electronic structure of iron corrolates, Accepted for publication
35. David Goldberg, Johns Hopkins, High-valent transition metal corrolazines, Accepted for publication
36. Roger Guilard, Dijon, and Karl Kadish, Houston, Cobalt face-to-face corroles, Accepted for publication

37. Christopher Ziegler, Akron, Ohio, High-valent N-confused porphyrins, Accepted for publication

High-valent Mn, Ni, and Cu
38. Charles Riordan, Delaware, High-valent NiO intermediates, Running late
39. Gary Brudvig, Yale, Photosystem II models, Accepted for publication
40. Sunney Chan, Taiwan, pMMO, Accepted for publication





Some technical notes on preparing your contribution

(1) First, regarding the length of your article, you have wide freedom, say anywhere from 8-10 to 30-50 printed pages, depending on the scope of your article.

(2) Your review articles are expected to be useful works of reference. Therefore, please prepare your tabular materials with care (whether they are Mössbauer parameters, NMR isotropic shifts, resonance Raman data or something else).

(3) Please also pay attention to Figures and other graphical materials. Elsevier pays for essential - as opposed to simply cosmetic - color so well-designed color figures are welcome.

(4) If you use ChemDraw to draw your structures, you might want to follow the settings recommended by JACS, JOC or IC. Please make sure that your atom labels are not too big or too small compared with the bond lengths and that your bond widths are not too thin or thick compared with the bond lengths. Use bold text with caution so it does not appear too "loud" compared with the rest of the figure. Importantly, for stylistic uniformity throughout the volume, please use Arial or Helvetica as the only fonts within figures and plots.

(5) Lastly, for esthetic purposes, we should probably agree on some common notation for formulas for the entire volume.
(a) Oxidation states should be shown as Roman superscripts everywhere, not within parentheses. E.g., Fe^IV complexes, Fe^IV O intermediates, Fe^IV(ProtoP)(O)(His), etc.
(b) Except for monatomic ligands, ligand names should generally be included in parentheses. Overall charges should be indicated as a superscript after enclosing the formula in square brackets. e.g. Fe(TDCPP)Cl, [Fe^IV(5-Me-TPA)(O)(OH)]⁺, etc.
(c) Place the metal first in the formulas of synthetic complexes. (This is an important source of stylistic nonuniformity in the literature.) Thus, Fe(OEP)Cl, rather than (OEP)FeCl. However, proteins are allowed as exceptions, e.g. MbFe^IVO.
(d) Use a reasonable mix of capital and small letters for ligand abbreviations. E.g. OEP (not oep), TPA (not tpa), 5-Me-TPA (not 5-me-tpa).
(e) Some recommended abbreviations: P = the porphine ligand (used in many theoretical studies), Por = a generic porphyrin, etc.

(In case you wonder where these dictatorial recommendations came from, they are a largely a combination of the conventions used by ACS journals and The Porphyrin Handbook!)