The effect of hip flexion angle on muscle elongation of the hip adductor muscles during stretching.

In order to perform effective static stretching of the hip adductor muscles, it is necessary to clarify the position where the muscles are most stretched. However, the effective flexion angle in stretching for each adductor muscle remains unclear. The goal of this study was to investigate the effect of hip flexion angle on muscle elongation of hip adductor muscles during stretching.

Biochemical studies of a soxF-encoded monomeric flavoprotein purified from the green sulfur bacterium Chlorobaculum tepidum that stimulates in vitro thiosulfate oxidation.

In the green sulfur bacterium Chlorobaculum tepidum, three sulfur oxidizing enzyme system (Sox) proteins, SoxAXK, SoxYZ, and SoxB (the core TOMES, thiosulfate oxidizing multi-enzyme system) are essential to in vitro thiosulfate oxidation. We purified monomeric flavoprotein SoxF from this bacterium, which had sulfide dehydrogenase activity. SoxF enhanced the thiosulfate oxidation activity of the purified core TOMES with various cytochromes as electron acceptors to different degrees without any change in the affinity for thiosulfate.

An overview on chlorophylls and quinones in the photosystem I-type reaction centers.

Minor but key chlorophylls (Chls) and quinones in photosystem (PS) I-type reaction centers (RCs) are overviewed in regard to their molecular structures. In the PS I-type RCs, the prime-type chlorophylls, namely, bacteriochlorophyll (BChl) a' in green sulfur bacteria, BChl g' in heliobacteria, Chl a' in Chl a-type PS I, and Chl d' in Chl d-type PS I, function as the special pairs, either as homodimers, (BChl a')(2) and (BChl g')(2) in anoxygenic organisms, or heterodimers, Chl a/a' and Chl d/d' in oxygenic photosynthesis. Conversions of BChl g to Chl a and Chl a to Chl d take place spontaneously under mild condition in vitro.

Inorganic sulfur oxidizing system in green sulfur bacteria.

Green sulfur bacteria use various reduced sulfur compounds such as sulfide, elemental sulfur, and thiosulfate as electron donors for photoautotrophic growth. This article briefly summarizes what is known about the inorganic sulfur oxidizing systems of these bacteria with emphasis on the biochemical aspects. Enzymes that oxidize sulfide in green sulfur bacteria are membrane-bound sulfide-quinone oxidoreductase, periplasmic (sometimes membrane-bound) flavocytochrome c sulfide dehydrogenase, and monomeric flavocytochrome c (SoxF).

Characterization of cytosolic tetrapyrrole-binding proteins in Arabidopsis thaliana.

In plant cells, tetrapyrroles are synthesized in plastids and distributed to numerous organelles to function in various vital activities. However, molecular mechanisms of tetrapyrroles trafficking in plant cells are poorly understood. In animal cells, experimental evidence suggests that the p22HBP/SOUL family are cytosolic heme carrier proteins functioning in heme trafficking.

SoxAX binding protein, a novel component of the thiosulfate-oxidizing multienzyme system in the green sulfur bacterium Chlorobium tepidum.

From the photosynthetic green sulfur bacterium Chlorobium tepidum (pro synon. Chlorobaculum tepidum), we have purified three factors indispensable for the thiosulfate-dependent reduction of the small, monoheme cytochrome c(554). These are homologues of sulfur-oxidizing (Sox) system factors found in various thiosulfate-oxidizing bacteria.

NB-protein (BchN-BchB) of dark-operative protochlorophyllide reductase is the catalytic component containing oxygen-tolerant Fe-S clusters.

Dark-operative protochlorophyllide (Pchlide) oxidoreductase is a nitrogenase-like enzyme consisting of the two components, L-protein (BchL-dimer) and NB-protein (BchN-BchB-heterotetramer). Here, we show that NB-protein is the catalytic component with Fe-S clusters. NB-protein purified from Rhodobacter capsulatus bound Pchlide that was readily converted to chlorophyllide a upon the addition of L-protein and Mg-ATP.