Journal of Inorganic Biochemistry – Karlin Special Issue

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Copper and other nonheme (Ni, Fe, & Mn) systems

Naturally, nonheme copper complexes and model systems are well-represented in this special issue! Blackburn and coworkers (https://doi.org/10.1016/j.jinorgbio.2022.111780) present a short review article to examine whether the current consensus mechanisms for the reactions of copper monooxygenases with molecular oxygen and the subsequent prediction of catalytic steps, were consistent with experimental observations on the enzymes themselves. The authors conclude that an alternative mechanism

Production and consumption of NO at heme and non-heme centers

Nitric oxide (NO) is a signaling molecule that regulates important physiological functions and is also involved in many pathological events. It has long been known that NO is biosynthesized from L-arginine and O2 by nitric oxide synthases. However, recent studies recognize that the non-canonical pathway for NO production, the nitrate-nitrite-NO pathway, is a major source of NO production under hypoxia. At least ten different heme proteins have been discovered with nitrite reductase-like

Heme-O2 and Heme-H2O2 chemistry

Previous studies have shown that both monohalophenols and trihalophenols are peroxidase substrates for the multifunctional catalytic hemoglobin dehaloperoxidase (DHP) from A. ornata. In the present study, Ghiladi and co-workers (https://doi.org/10.1016/j.jinorgbio.2022.111944) employed dihalophenols in mechanistic and structural studies of DHP, and demonstrated both oxygenation (via peroxygenase activity) and oxidative dehalogenation (via peroxidase activity) by two simultaneous pathways for

Native and artificial metalloprotein design

Metalloproteins are key players in a huge range of biochemical pathways, and post-translational modifications such as phosphorylation can impact their functionality. Phosphorylation studies have traditionally focused on residues such as serine, threonine, and tyrosine, and our understanding of the role(s) that histidine phosphorylation plays is, by way of comparison, relatively minimal. A contribution by Mathis and Barrios (https://doi.org/10.1016/j.jinorgbio.2021.111606) provides an in-depth

Metals in human health and disease

Prion disease is an infectious neurodegenerative disorder characterized by the accumulation of a misfolded form of the prion protein. The cellular prion protein (PrPC) is a membrane-anchored copper-binding protein that undergoes proteolytic processing. Sánchez-López and Quintanar (https://doi.org/10.1016/j.jinorgbio.2021.111686) report their studies on β-cleavage of PrPC, which is associated with pathogenic conditions and results in two proteolytic fragments, one of which has a free N-terminal

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