Handling of the Bivalve , Endangered and Pathogen-Affected Species, for Controlled Reproduction: Precautions Taken.

Following the increased mass mortality of populations in the Mediterranean, reliable protocols for the transport, maintenance, and controlled reproduction of this highly endangered species were drawn up within the European Life Pinna project. To test these protocols, the large Pinnidae , which shares similar habits to , has been used. In December 2022, a transport trial of nine specimens of from Trieste (NE Italy) to Camogli (NW Italy) was carried out.

Hydrogen evolution from water catalyzed by cobalt-mimochrome VI*a, a synthetic mini-protein.

A synthetic enzyme is reported that electrocatalytically reduces protons to hydrogen (H) in water near neutral pH under aerobic conditions. Cobalt mimochrome VI*a (CoMC6*a) is a mini-protein with a cobalt deuteroporphyrin active site within a scaffold of two synthetic peptides covalently bound to the porphyrin. Comparison of the activity of CoMC6*a to that of cobalt microperoxidase-11 (CoMP11-Ac), a cobalt porphyrin catalyst with a single "proximal" peptide and no organized secondary structure, reveals that CoMC6*a has significantly enhanced longevity, yielding a turnover number exceeding 230 000, in comparison to 25 000 for CoMP11-Ac.

PCV13 vaccination impact: A multicenter study of pneumonia in 10 pediatric hospitals in Argentina.

Introduction: In 2012, PCV13 was introduced into the National Immunization Program in Argentina, 2+1 schedule for children <2 years. Coverage rates for 1st and 3rd doses were 69% and 41.0% in 2012, 98% and 86% in 2013; 99% and 89% in 2014, respectively.

Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design.

Rational design provides an attractive strategy to tune and control the reactivity of bioinspired catalysts. Although there has been considerable progress in the design of heme oxidase mimetics with active-site environments of ever-growing complexity and catalytic efficiency, their stability during turnover is still an open challenge. Herein, we show that the simple incorporation of two 2-aminoisobutyric acids into an artificial peptide-based peroxidase results in a new catalyst (Fe -MC6*a) with higher resistance against oxidative damage and higher catalytic efficiency.

Oxidation catalysis by iron and manganese porphyrins within enzyme-like cages.

Inspired by natural heme-proteins, scientists have attempted for decades to design efficient and selective metalloporphyrin-based oxidation catalysts. Starting from the pioneering work on small molecule mimics in the late 1970s, we have assisted to a tremendous progress in designing cages of different nature and complexity, able to accommodate metalloporphyrins. With the intent of tuning and controlling their reactivity, more and more sophisticated and diverse environments are continuously exploited.