Ferredoxin (Fd) is a small soluble iron-sulfur protein essential in almost all oxygenic photosynthetic organisms. It contains a single [2Fe-2S] cluster coordinated by four cysteine ligands. It accepts electrons from the stromal surface of PSI and facilitates transfer to a myriad of acceptors involved in diverse metabolic processes, including generation of NADPH via Fd-NADP-reductase, cyclic electron transport for ATP synthesis, nitrate reduction, nitrite reductase, sulfite reduction, hydrogenase and other reductive reactions. Fd serves as the central hub for these diverse cellular reactions and is integral to complex cellular metabolic networks. We describe advances on the central role of Fd and its evolutionary role from cyanobacteria to algae/plants. We compare structural diversity of Fd partners to understand this orchestrating role and shed light on how Fd dynamically partitions between competing partner proteins to enable the optimum transfer of PSI-derived electrons to support cell growth and metabolism., J. Mondal, B. D. Bruce., and Obsahuje bibliografické odkazy
The paper describes the general form of functional-differential equations of the first order with $m (m\ge 1)$ delays which allows nontrivial global transformations consisting of a change of the independent variable and of a nonvanishing factor. A functional equation \[ f(t, uv, u_{1}v_{1}, \ldots , u_{m}v_{m}) = f(x, v, v_{1}, \ldots , v_{m})g(t, x, u, u_{1}, \ldots , u_{m})u + h(t, x, u, u_{1}, \ldots , u_{m})v \] for $u\ne 0$ is solved on $\mathbb R$ and a method of proof by J. Aczél is applied.