Sedimentary Cobalt Protoporphyrin as a Potential Precursor of Prosthetic Heme Group for Bacteria Inhabiting Fossil Organic Matter-Rich Shale Rock

This study hypothesizes that bacteria inhabiting shale rock affect the content of the sedimentary cobalt protoporphyrin present in it and can use it as a precursor for heme synthesis. To verify this hypothesis, we conducted qualitative and quantitative comparative analyses of cobalt protoporphyrin as well as heme, and heme iron in shale rock that were (i) inhabited by bacteria in the field, (ii) treated with bacteria in the laboratory, and with (iii) bacterial culture on synthetic cobalt protoporphyrin. Additionally, we examined the above-mentioned samples for the presence of enzymes involved in the heme biosynthesis and uptake as well as hemoproteins. We found depletion of cobalt protoporphyrin and a much higher heme concentration in the shale rock inhabited by bacteria in the field as well as the shale rock treated with bacteria in the laboratory. Similarly, we observed the accumulation of protoporphyrin in bacterial cells grown on synthetic cobalt protoporphyrin. We detected numerous hemoproteins in metaproteome of bacteria inhabited shale rock in the field and in proteomes of bacteria inhabited shale rock and synthetic cobalt protoporhyrin in the laboratory, but none of them had all the enzymes involved in the heme biosynthesis. However, proteins responsible for heme uptake, ferrochelatase and sirohydrochlorin cobaltochelatase/sirohydrochlorin cobalt-lyase were detected in all studied samples.

The globin superfamily: functions in nitric oxide formation and decay

Globin proteins are ubiquitous in living organisms and carry out a variety of functions related to the ability of their prosthetic heme group to bind gaseous ligands, such as oxygen, nitric oxide (NO), and CO. Moreover, they catalyze important reactions with nitrogen oxide species, such as NO dioxygenation and nitrite reduction. The formation of NO from nitrite is a reaction catalyzed by globins that has received increasing attention due to its potential as a hypoxic NO signaling mechanism. In this review, we revisit the current knowledge about the role of globins in NO formation and its physiological implications.

Histolysis, Histogenesis, and Differentiation during Insect Metamorphosis in Relation to Metabolic Changes

The most obvious change in metabolism during the more advanced type of insect metamorphosis is the change in the integral metabolic activity. After pupation there is first a marked decrease and later an increase of, for instance, the oxygen consumption. The respiratory metabolic curve is U-shaped. The cause of this change is a corresponding variation in the activity of oxidative enzyme systems. If one compares the variation of the spontaneous Mb-reduction and of the oxygen consumption in the fly Calliphora, one finds that the two curves have almost the same course (Agrell, 1947b). This shows an important co-operation of the dehydrogenase systems. The cytochrome system also shows a similar U-shaped variation during the period of metamorphosis, according to Wolsky (1938), Williams (1948) and Sacktor (1950). One limiting factor is the protein part of the enzymes, which is first broken down and later rebuilt (Agrell, 1946). Another limiting factor is the prosthetic heme group in the cytochromes (Williams, 1951).