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Photosynthesis, respiration and ATP/ADP are related.

The energy for ATP synthesis comes from organic molecules (such as carbohydrates), or from sunlight, or from inorganic electron donors. We can classify organisms according to their source of energy and organic carbon:

Half beans will be used to represent ATP synthetase molecules.

The proton-motive force is a combination of a difference in proton (H+ ion) concentrations across a membrane, and the resulting electrical potential. All prokaryotic cells (Bacteria and Archaea) maintain a proton gradient (pH gradient) across their plasma membranes. Mitochondria maintain a proton gradient across the inner mitochondrial membrane. The interior of the bacterial cell (or the mitochondrial matrix) is relatively alkaline, whereas the exterior periplasmic space (or the mitochondrial intermembrane space) is relatively acidic. Because protons are positively charged, an imbalance of protons also creates an electrical charge difference across the membrane. This proton motive force is a form of stored energy, and protons returning across the membrane down their concentration and electrical charge gradients release free energy that can be harnessed by ATP synthase to make ATP. The lipid bilayer membrane is almost impermeable to protons, so the proton gradient is stable and normally does not discharge except via ATP synthase, or via proton channels that may open in the membrane.

Animation of ATP Synthesis will be available on

(1994). Structure at2.8 Å resolution of F1-ATPase from bovine heart mitochondria.

Metabolic pathways carry out reactions that capture energy from these various sources (organic compounds, sunlight or chemicals) and couple them to synthesis of ATP from ADP.

*except in some phototrophic archaea that use bacteriorhodopsin to directly pump protons across the membrane using light energy – we’ll see that in the section on photosynthesis.

F1ATP Synthase – watch the video below and know this!

(1993).Thebinding change mechanism for ATP synthase - Some probabilitiesand possibilities.

A
similar activity can be used to create models of mitochondria.

Using tennis balls the students will play a game of catch to demonstrate
the loss of 1 phosphate to form ADP from ATP and the gain of one phosphate to
form ATP from ADP.

Overview

This lesson will examine herbicides that affect light-related cellular processes, thereby causing damage to plants. There are four basic mechanisms that will be studied: herbicides that inhibit or block synthesis of Protoporphyrin IX; herbicides that inhibit synthesis of carotenoids; herbicides that block Photosystem II electron transfer; and herbicides that divert electrons from Photosystem I. All share the ability to cause cellular damage in the presence of light.

Objectives

At the completion of this lesson, students will be able to differentiate between herbicides with modes of action based on:

Structure at 2.8 Åresolution of F1-ATPase from bovine heart mitochondria.
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ATP Synthase: The power plant of the cell - YouTube

V-ATPases (for ‘’)are found in the eukaryotic endomembrane system (vacuoles, Golgi apparatus,endosomes, lysosomes, clathrin-coated vesicles {transport external substancesinside the cell}, and plant tonolplasts), and in the plasma membrane ofprokaryotes and certain specialised eukaryotic cells. V-ATPases hydrolyse ATPto drive a proton pump, but cannot work in reverse to synthesize ATP.V-ATPases are involved in a variety of vitalintra- and inter-cellular processes such as receptor mediated endocytosis,protein trafficking, active transport of metabolites, homeostasis andneurotransmitter release

ATP Synthase Animation - Sumanas, Inc.

ATP production in the thylakoid membranes of chloroplasts and cyanobacteria as well as in the inner membranes of mitochondria and bacterial plasma membranes is catalyzed by ATP synthase, a complex, evolutionary conserved multi-subunit enzyme. Whereas ATP synthase was discovered already more than 40 years ago, the last 10–15 years have seen tremendous progress concerning structure determination of large parts of this enzyme. Mutagenesis studies based on this structural information have yielded hints on how this enzyme may couple the flow of protons along an electrochemical potential gradient across a bio-membrane to chemical synthesis of ATP. Single molecule measurements have proven a unique enzymatic mechanism for ATP synthase: catalysis coupled to and driven by rotary movement of individual subunits against others in the complex. As such, ATP synthase acts as a fascinating biological power station operating at nano-scale. Current open questions on rotary catalysis include transient storage of energy within the enzyme upon proton transport and the impact of rotor stochiometry on catalytic activity.

The ATP synthase operates through a ..

As production and even more consumption of ATP in most organisms must be tightly controlled, ATP synthase displays a number of mechanisms for regulation of the enzyme’s activity, allowing for adaptation to changing environmental conditions. This includes features generally found in ATP synthases such as the inhibition by Mg-ADP bound to the catalytic site or action of the inhibitory subunit ε, as well as specialized features such as an inserted regulatory region of ATP synthase from cyanobacteria and chloroplasts, which allows redox-regulation of activity in the chloroplast enzyme. Structural data and functional measurements have increased our understanding of ATP synthase regulation and the complex interplay between the mechanisms involved.

In the direction of ATP synthesis, ..

In this review, general structural and functional features of ATP synthase as well as properties characteristic for the cyanobacterial enzyme will be discussed.

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