酶催化过渡态能量图

一张简洁的物理化学/生化教科书能量图，横轴为反应坐标，纵轴为吉布斯自由能。未催化路径（暗红曲线）峰高标 "TS (uncatalysed)"，双向箭头注 "ΔG‡ (uncatalysed)"；酶催化路径（钴蓝曲线）峰低标 "TS (enzyme-bound)"，注 "ΔG‡ (enzyme)"。两曲线同起（灰色椭圆 「Reaction Coordinate」）同终（「Gibbs Free Energy (ΔG)」，橄榄绿 ΔG° 标注），酶曲线过渡态处淡蓝晕光。右下小插图：5 线极简风格的底物锁与酶钥匙结合示意。10pt 轴标，9pt 斜体曲线标注，无网格，白色背景。

A clean minimalist energy diagram comparing uncatalysed and enzyme-catalysed reaction pathways, styled for a physical chemistry or biochemistry textbook. The composition is centred on a horizontal reaction coordinate axis (x-axis, labelled "Reaction Coordinate") and a vertical free energy axis (y-axis, labelled "Gibbs Free Energy (ΔG)"). Two smooth curves overlap: the uncatalysed pathway in muted red peaks at a high transition state labelled "TS (uncatalysed)" with a dashed horizontal indicator and a double-headed arrow annotated "ΔG‡ (uncatalysed)". The enzyme-catalysed pathway in cobalt blue rises to a much lower peak labelled "TS (enzyme-bound)" with another dashed indicator and a smaller double-headed arrow annotated "ΔG‡ (enzyme)". Both curves share the same starting point ("Substrates") in a grey shaded oval and the same ending point ("Products") lower on the right, with the overall ΔG° reaction annotated in olive-green. The transition-state region of the enzyme curve is highlighted with a faint blue halo. A small inset schematic at lower-right shows substrate (lock) fitting into enzyme active site (key), drawn in 5-line minimalist style. Axis labels in 10 pt, curve labels in italic 9 pt. No grid lines, white background.