English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

A small molecule, hitherto called X, which is present in legume root nodules and ligates reversibly to the monomeric protein, leghemoglobin, with formation of a hemochrome structure, is identified as nicotinic acid. The binding constants at pH 5.3 are K = 7.3 x 10(5) M(-1) and K = 3.0 x 10(4) M(-1) for combination of nicotinic acid with ferric and ferrous leghemoglobin, respectively. This high affinity binding of ligand requires an unsubstituted pyridine ring nitrogen atom and an ionized carboxyl group in the 3-position of the ring. Binding of nicotinic acid is favored at acid pH and is reflected by diminished apparent affinity of leghemoglobin for oxygen.

Nicotinic Acid as a Ligand Affecting Leghemoglobin Structure and Oxygen Reactivity