Fifty years of inorganic biochemistry: Developments, trends, highlights, impact and citations.

A brief historic overview and analysis is presented of the almost 9000 scientific articles that have appeared in the Journal of Inorganic Biochemistry (JIB) and its predecessor (Bioinorganic Chemistry), since 1973. This overview has a focus on the different topics, in particular on the different elements of the Periodic Table and on papers that have received very large numbers of citations. Over the whole period, copper has been the element occurring in most publications (almost 1800, which is 20%), followed by iron which occurs in some 12% of all papers. Other favorite elements are zinc, platinum and ruthenium. The worldwide origin of papers published in JIB has been analyzed as well, showing a quite evenly worldwide distribution, with just a few exceptions. Trends in selected scientific topics over time (first 10 years; last 25 years, last 10 years) are also discussed. Also authors and institutes with the largest number of papers published in JIB have been detected. The numerical information is based on an analysis of the Web of Science with a cutoff date around July 1, 2020.

Bert Lester Vallee: a lasting legacy.

The enlightened formation, by Bert and Kuggie Vallee, of a procedure whereby senior scientists spend short time of about a month at Harvard, Oxford and other institutions, is illustrated by the views and opinions of those selected.

An appreciation of William H. Orme-Johnson III.

This short memoir of personal and professional interactions with Bill Orme-Johnson covers a period of more than 35 years. Included are reflections on the early history of copper oxidases, iron-sulfur proteins and nitrogenase.

Invited award contribution for ACS Award in Inorganic Chemistry. Geometric and electronic structure contributions to function in bioinorganic chemistry: active sites in non-heme iron enzymes.

Spectroscopy has played a major role in the definition of structure/function correlations in bioinorganic chemistry. The importance of spectroscopy combined with electronic structure calculations is clearly demonstrated by the non-heme iron enzymes. Many members of this large class of enzymes activate dioxygen using a ferrous active site that has generally been difficult to study with most spectroscopic methods. A new spectroscopic methodology has been developed utilizing variable temperature, variable field magnetic circular dichroism, which enables one to obtain detailed insight into the geometric and electronic structure of the non-heme ferrous active site and probe its reaction mechanism on a molecular level. This spectroscopic methodology is presented and applied to a number of key mononuclear non-heme iron enzymes leading to a general mechanistic strategy for O2 activation. These studies are then extended to consider the new features present in the binuclear non-heme iron enzymes and applied to understand (1) the mechanism of the two electron/coupled proton transfer to dioxygen binding to a single iron center in hemerythrin and (2) structure/function correlations over the oxygen-activating enzymes stearoyl-ACP Delta9-desaturase, ribonucleotide reductase, and methane monooxygenase. Electronic structure/reactivity correlations for O2 activation by non-heme relative to heme iron enzymes will also be developed.