Corrigendum: Differences in Bioenergetic Metabolism of Obligately Alkaliphilic Under High pH Depend on the Aeration Conditions.

[This corrects the article DOI: 10.3389/fmicb.2022.

Differences in Bioenergetic Metabolism of Obligately Alkaliphilic Under High pH Depend on the Aeration Conditions.

Alkaliphilic appear to produce ATP based on the H-based chemiosmotic theory. However, the bulk-based chemiosmotic theory cannot explain the ATP production in alkaliphilic bacteria because the H concentration required for driving ATP synthesis through the ATPase does not occur under the alkaline conditions. Alkaliphilic bacteria produce ATP in an H-diluted environment by retaining scarce H extruded by the respiratory chain on the outer surface of the membrane and increasing the potential of the H for ATP production on the outer surface of the membrane using specific mechanisms of ATP production.

Formation of Proton Motive Force Under Low-Aeration Alkaline Conditions in Alkaliphilic Bacteria.

In Mitchell's chemiosmotic theory, a proton (H) motive force across the membrane (Δp), generated by the respiratory chain, drives FF-ATPase for ATP production in various organisms. The bulk-base chemiosmotic theory cannot account for ATP production in alkaliphilic bacteria. However, alkaliphiles thrive in environments with a H concentrations that are one-thousandth (ca.

A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential.

A membrane-anchored cytochrome c-550, which is highly expressed in obligately alkaliphilic Bacillus clarkii K24-1U, was purified and characterized. The protein contained a conspicuous sequence of Gly(22)-Asn(34), in comparison with the other Bacillus small cytochromes c. Analytical data indicated that the original and lipase-treated intermediate forms of cytochrome c-550 bind to fatty acids of C(15), C(16) and C(17) chain lengths and C(15) chain length, respectively, and it was considered that these fatty acids are bound to glycerol-Cys(18).